This%32BioPAX%32Level%322%32output%32for%32organism%32MetaCyc%44%32pathway%32superpathway%3732of%3732phenylalanine%3744%3732tyrosine%3744%3732and%3732tryptophan%3732biosynthesis%10was%32automatically%32generated%32from%32URL%32http%58%47%47BioCyc%46org%47META%47pathway%45biopax%63type%612%3738object%61COMPLETE%45ARO%45PWY%32on%3229%45May%452009%32%3202%5804%5825%46%32%32Note%32that%32all%32IDs%32are%32auto%45generated%44%10and%32are%32valid%32in%32the%32scope%32of%32this%32file%32only%46%32%32If%32the%32data%32is%32regenerated%32at%32some%32later%10time%44%32or%32data%32for%32another%32pathway%32is%32generated%32from%32this%32same%32site%44%32there%32are%32no%32%10guarantees%32that%32the%32same%32IDs%32will%32refer%32to%32the%32same%32objects%46%32%32To%32retrieve%32a%32file%32%10containing%32a%32complete%32list%32of%32pathways%32for%32this%32organism%32in%32BioPAX%32format%44%32please%10visit%32http%58%47%47biocyc%46org%47download%45flatfiles%46shtml reduced flavin cellular_component unknown GO GO:0008372 1 Chorismate synthase catalyzes the final reaction in chorismate biosynthesis. The enzyme is associated with NADPH-dependent flavin reductase and dehydroquinate synthase. Chorismate synthase requires NADPH-dependent flavin reductase, Mg<SUP>2+</SUP>, NADPH and flavin (FMN or FAD) for activity. The flavin reductase provides the reduced flavin cofactor used by chorismate synthase. |CITS: [97285]| 4.2.3.5 320.149 5-enolpyruvyl-shikimate-3-phosphate CML <cml> <molecule id="3-ENOLPYRUVYL-SHIKIMATE-5P" title="5-enolpyruvyl-shikimate-3-phosphate" dictRef="dict3-ENOLPYRUVYL-SHIKIMATE-5P"> <atomArray> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom1" elementType="O" x2="-24036.0" y2="-19515.0" formalCharge="-1"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom2" elementType="O" x2="-9599.0" y2="-4046.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom3" elementType="O" x2="-9599.0" y2="-11820.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom4" elementType="O" x2="-3411.0" y2="-2063.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom5" elementType="C" x2="-9599.0" y2="793.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom6" elementType="C" x2="-16580.0" y2="-8568.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom7" elementType="C" x2="4046.0" y2="793.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom8" elementType="C" x2="11185.0" y2="-8568.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom9" elementType="C" x2="19435.0" y2="-8568.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom10" elementType="O" x2="23957.0" y2="-1666.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom11" elementType="O" x2="-635.0" y2="-6822.0" formalCharge="-1"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom12" elementType="C" x2="-16818.0" y2="-19435.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom13" elementType="O" x2="-16580.0" y2="-14755.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom14" elementType="P" x2="-4760.0" y2="-5394.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom15" elementType="C" x2="-20070.0" y2="-17135.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom16" elementType="C" x2="4046.0" y2="-17690.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom17" elementType="C" x2="-9599.0" y2="-17690.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom18" elementType="C" x2="-16738.0" y2="-24036.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom19" elementType="O" x2="-6346.0" y2="-8805.0" formalCharge="-1"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom20" elementType="O" x2="-20149.0" y2="-12375.0"/> <atom id="3-ENOLPYRUVYL-SHIKIMATE-5P-atom21" elementType="O" x2="22370.0" y2="-16024.0" formalCharge="-1"/> </atomArray> <bondArray> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond1" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom21 3-ENOLPYRUVYL-SHIKIMATE-5P-atom9" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond2" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom20 3-ENOLPYRUVYL-SHIKIMATE-5P-atom15" order="2"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond3" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom19 3-ENOLPYRUVYL-SHIKIMATE-5P-atom14" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond4" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom18 3-ENOLPYRUVYL-SHIKIMATE-5P-atom12" order="2"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond5" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom16 3-ENOLPYRUVYL-SHIKIMATE-5P-atom17" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond6" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom15 3-ENOLPYRUVYL-SHIKIMATE-5P-atom12" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond7" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom14 3-ENOLPYRUVYL-SHIKIMATE-5P-atom2" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond8" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom13 3-ENOLPYRUVYL-SHIKIMATE-5P-atom6" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond9" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom12 3-ENOLPYRUVYL-SHIKIMATE-5P-atom3" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond10" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom11 3-ENOLPYRUVYL-SHIKIMATE-5P-atom14" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond11" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom10 3-ENOLPYRUVYL-SHIKIMATE-5P-atom9" order="2"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond12" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom9 3-ENOLPYRUVYL-SHIKIMATE-5P-atom8" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond13" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom8 3-ENOLPYRUVYL-SHIKIMATE-5P-atom16" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond14" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom8 3-ENOLPYRUVYL-SHIKIMATE-5P-atom7" order="2"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond15" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom7 3-ENOLPYRUVYL-SHIKIMATE-5P-atom5" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond16" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom6 3-ENOLPYRUVYL-SHIKIMATE-5P-atom5" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond17" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom6 3-ENOLPYRUVYL-SHIKIMATE-5P-atom17" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond18" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom4 3-ENOLPYRUVYL-SHIKIMATE-5P-atom14" order="2"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond19" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom3 3-ENOLPYRUVYL-SHIKIMATE-5P-atom17" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond20" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom2 3-ENOLPYRUVYL-SHIKIMATE-5P-atom5" order="1"/> <bond id="3-ENOLPYRUVYL-SHIKIMATE-5P-bond21" atomRefs="3-ENOLPYRUVYL-SHIKIMATE-5P-atom1 3-ENOLPYRUVYL-SHIKIMATE-5P-atom15" order="1"/> </bondArray> <formula concise="C 10 H 9 O 10 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">320.149</float> <string title="smiles">C(C1(=CC(OP(=O)([O-])[O-])C(C(OC(C([O-])=O)=C)C1)O))(=O)[O-]</string> </molecule> </cml> EPSP 3-enolpyruvyl-shikimate-5-phosphate 3-enolpyruvyl-shikimate-5-P 5-O-(1-carboxyvinyl)-3-phosphoshikimate MetaCyc 3-ENOLPYRUVYL-SHIKIMATE-5P LIGAND C01269 CCO-CYTOPLASM GO GO:0005737 1 Chorismate synthase 95.979 phosphate CML <cml> <molecule id="Pi" title="phosphate" dictRef="dictPi"> <atomArray> <atom id="Pi-atom1" elementType="P" x2="-1400.0" y2="-1400.0"/> <atom id="Pi-atom2" elementType="O" x2="823600.0" y2="-1400.0" formalCharge="-1"/> <atom id="Pi-atom3" elementType="O" x2="-1400.0" y2="823600.0" formalCharge="-1"/> <atom id="Pi-atom4" elementType="O" x2="-1400.0" y2="-826400.0"/> <atom id="Pi-atom5" elementType="O" x2="-826400.0" y2="-1400.0"/> </atomArray> <bondArray> <bond id="Pi-bond1" atomRefs="Pi-atom5 Pi-atom1" order="2"/> <bond id="Pi-bond2" atomRefs="Pi-atom4 Pi-atom1" order="1"/> <bond id="Pi-bond3" atomRefs="Pi-atom3 Pi-atom1" order="1"/> <bond id="Pi-bond4" atomRefs="Pi-atom2 Pi-atom1" order="1"/> </bondArray> <formula concise="H 1 O 4 P 1" formalCharge="-3"/> <float title="molecularWeight" units="g/mol">95.979</float> <string title="smiles">P([O-])([O-])(O)=O</string> </molecule> </cml> inorganic phosphate phosphate-inorganic Pi orthophosphate PO<SUB>4</SUB><SUP>3-</SUP> HPO<SUB>4</SUB><SUP>2-</SUP> HPO<SUB>4</SUB><SUP>-2</SUP> MetaCyc Pi CAS 14265-44-2 LIGAND C00009 1 224.17 chorismate CML <cml> <molecule id="CHORISMATE" title="chorismate" dictRef="dictCHORISMATE"> <atomArray> <atom id="CHORISMATE-atom1" elementType="C" x2="0.0" y2="-1.2375e+7"/> <atom id="CHORISMATE-atom2" elementType="C" x2="0.0" y2="-2.0625e+7"/> <atom id="CHORISMATE-atom3" elementType="C" x2="1.429e+7" y2="-1.2375e+7"/> <atom id="CHORISMATE-atom4" elementType="C" x2="1.429e+7" y2="-2.0625e+7"/> <atom id="CHORISMATE-atom5" elementType="O" x2="-3000.0" y2="-3.7125e+7"/> <atom id="CHORISMATE-atom6" elementType="O" x2="1.4287e+7" y2="-3.7125e+7" formalCharge="-1"/> <atom id="CHORISMATE-atom7" elementType="C" x2="7142000.0" y2="-3.3e+7"/> <atom id="CHORISMATE-atom8" elementType="C" x2="7142000.0" y2="-2.475e+7"/> <atom id="CHORISMATE-atom9" elementType="C" x2="7142000.0" y2="-8250000.0"/> <atom id="CHORISMATE-atom10" elementType="O" x2="7142000.0" y2="0.0"/> <atom id="CHORISMATE-atom11" elementType="O" x2="2.1432e+7" y2="-8250000.0"/> <atom id="CHORISMATE-atom12" elementType="C" x2="2.858e+7" y2="-1.2375e+7"/> <atom id="CHORISMATE-atom13" elementType="C" x2="2.858e+7" y2="-2.0625e+7"/> <atom id="CHORISMATE-atom14" elementType="C" x2="3.5723e+7" y2="-8250000.0"/> <atom id="CHORISMATE-atom15" elementType="O" x2="3.5723e+7" y2="0.0"/> <atom id="CHORISMATE-atom16" elementType="O" x2="4.2699e+7" y2="-1.2374001e+7" formalCharge="-1"/> </atomArray> <bondArray> <bond id="CHORISMATE-bond1" atomRefs="CHORISMATE-atom8 CHORISMATE-atom4" order="2"/> <bond id="CHORISMATE-bond2" atomRefs="CHORISMATE-atom3 CHORISMATE-atom4" order="1"/> <bond id="CHORISMATE-bond3" atomRefs="CHORISMATE-atom3 CHORISMATE-atom11" order="1"/> <bond id="CHORISMATE-bond4" atomRefs="CHORISMATE-atom12 CHORISMATE-atom11" order="1"/> <bond id="CHORISMATE-bond5" atomRefs="CHORISMATE-atom14 CHORISMATE-atom16" order="1"/> <bond id="CHORISMATE-bond6" atomRefs="CHORISMATE-atom14 CHORISMATE-atom12" order="1"/> <bond id="CHORISMATE-bond7" atomRefs="CHORISMATE-atom2 CHORISMATE-atom8" order="1"/> <bond id="CHORISMATE-bond8" atomRefs="CHORISMATE-atom9 CHORISMATE-atom3" order="1"/> <bond id="CHORISMATE-bond9" atomRefs="CHORISMATE-atom1 CHORISMATE-atom2" order="2"/> <bond id="CHORISMATE-bond10" atomRefs="CHORISMATE-atom1 CHORISMATE-atom9" order="1"/> <bond id="CHORISMATE-bond11" atomRefs="CHORISMATE-atom8 CHORISMATE-atom7" order="1"/> <bond id="CHORISMATE-bond12" atomRefs="CHORISMATE-atom7 CHORISMATE-atom5" order="2"/> <bond id="CHORISMATE-bond13" atomRefs="CHORISMATE-atom7 CHORISMATE-atom6" order="1"/> <bond id="CHORISMATE-bond14" atomRefs="CHORISMATE-atom9 CHORISMATE-atom10" order="1"/> <bond id="CHORISMATE-bond15" atomRefs="CHORISMATE-atom12 CHORISMATE-atom13" order="2"/> <bond id="CHORISMATE-bond16" atomRefs="CHORISMATE-atom14 CHORISMATE-atom15" order="2"/> </bondArray> <formula concise="C 10 H 8 O 6" formalCharge="0"/> <float title="molecularWeight" units="g/mol">224.17</float> <string title="smiles">C([O-])(=O)C1(C=CC(O)C(OC(=C)C(=O)[O-])C=1)</string> </molecule> </cml> chorismic acid MetaCyc CHORISMATE LIGAND C00251 CAS 55508-12-8 1 5-enolpyruvylshikimate-3-phosphate phospholyase MetaCyc CHORISMATE-SYNTHASE-RXN UniProt Q12640 UniProt O74413 UniProt P12008 RELATED-TO UniProt P16280 UniProt Q42884 UniProt Q42885 UniProt P28777 UniProt Q9CET2 UniProt Q9PM41 UniProt P43875 UniProt Q58575 UniProt Q9JT81 UniProt P23353 UniProt P27793 AROFBACSU-MONOMER Bacillus subtilis NCBI Taxonomy 1423 AroF vegetative protein 216 veg216 MetaCyc AROFBACSU-MONOMER 1 REVERSIBLE chorismate synthase 5-enolpyruvylshikimate-3-phosphate phospholyase 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase MetaCyc ENZRXN-1481 456.348 FMNH2 CML <cml> <molecule id="FMNH2" title="FMNH2" dictRef="dictFMNH2"> <atomArray> <atom id="FMNH2-atom1" elementType="O" x2="-80240.0" y2="31640.0"/> <atom id="FMNH2-atom2" elementType="P" x2="150310.0" y2="231680.0"/> <atom id="FMNH2-atom3" elementType="O" x2="150310.0" y2="313050.0"/> <atom id="FMNH2-atom4" elementType="C" x2="157090.0" y2="-231680.0"/> <atom id="FMNH2-atom5" elementType="O" x2="157090.0" y2="-314180.0"/> <atom id="FMNH2-atom6" elementType="C" x2="-160480.0" y2="-72330.0"/> <atom id="FMNH2-atom7" elementType="O" x2="309660.0" y2="-76850.0"/> <atom id="FMNH2-atom8" elementType="O" x2="-80240.0" y2="96060.0"/> <atom id="FMNH2-atom9" elementType="C" x2="235070.0" y2="-111890.0"/> <atom id="FMNH2-atom10" elementType="C" x2="2260.0" y2="167260.0"/> <atom id="FMNH2-atom11" elementType="C" x2="2260.0" y2="31640.0"/> <atom id="FMNH2-atom12" elementType="C" x2="-313050.0" y2="-235070.0"/> <atom id="FMNH2-atom13" elementType="C" x2="-242980.0" y2="-111890.0"/> <atom id="FMNH2-atom14" elementType="C" x2="53110.0" y2="-21470.0"/> <atom id="FMNH2-atom15" elementType="C" x2="-242980.0" y2="-194390.0"/> <atom id="FMNH2-atom16" elementType="C" x2="2260.0" y2="231680.0"/> <atom id="FMNH2-atom17" elementType="C" x2="2260.0" y2="96060.0"/> <atom id="FMNH2-atom18" elementType="O" x2="-80240.0" y2="167260.0"/> <atom id="FMNH2-atom19" elementType="N" x2="157090.0" y2="-72330.0"/> <atom id="FMNH2-atom20" elementType="C" x2="-314180.0" y2="-72330.0"/> <atom id="FMNH2-atom21" elementType="O" x2="231680.0" y2="231680.0" formalCharge="-1"/> <atom id="FMNH2-atom22" elementType="N" x2="-2260.0" y2="-231680.0"/> <atom id="FMNH2-atom23" elementType="N" x2="235070.0" y2="-194390.0"/> <atom id="FMNH2-atom24" elementType="C" x2="-84760.0" y2="-111890.0"/> <atom id="FMNH2-atom25" elementType="O" x2="80240.0" y2="231680.0"/> <atom id="FMNH2-atom26" elementType="N" x2="-2260.0" y2="-72330.0"/> <atom id="FMNH2-atom27" elementType="C" x2="-160480.0" y2="-231680.0"/> <atom id="FMNH2-atom28" elementType="O" x2="150310.0" y2="150310.0" formalCharge="-1"/> <atom id="FMNH2-atom29" elementType="C" x2="77980.0" y2="-194390.0"/> <atom id="FMNH2-atom30" elementType="C" x2="77980.0" y2="-111890.0"/> <atom id="FMNH2-atom31" elementType="C" x2="-84760.0" y2="-194390.0"/> </atomArray> <bondArray> <bond id="FMNH2-bond1" atomRefs="FMNH2-atom31 FMNH2-atom24" order="1"/> <bond id="FMNH2-bond2" atomRefs="FMNH2-atom30 FMNH2-atom29" order="2"/> <bond id="FMNH2-bond3" atomRefs="FMNH2-atom30 FMNH2-atom26" order="1"/> <bond id="FMNH2-bond4" atomRefs="FMNH2-atom29 FMNH2-atom4" order="1"/> <bond id="FMNH2-bond5" atomRefs="FMNH2-atom29 FMNH2-atom22" order="1"/> <bond id="FMNH2-bond6" atomRefs="FMNH2-atom28 FMNH2-atom2" order="1"/> <bond id="FMNH2-bond7" atomRefs="FMNH2-atom27 FMNH2-atom31" order="2"/> <bond id="FMNH2-bond8" atomRefs="FMNH2-atom26 FMNH2-atom14" order="1"/> <bond id="FMNH2-bond9" atomRefs="FMNH2-atom25 FMNH2-atom2" order="1"/> <bond id="FMNH2-bond10" atomRefs="FMNH2-atom24 FMNH2-atom6" order="2"/> <bond id="FMNH2-bond11" atomRefs="FMNH2-atom24 FMNH2-atom26" order="1"/> <bond id="FMNH2-bond12" atomRefs="FMNH2-atom23 FMNH2-atom9" order="1"/> <bond id="FMNH2-bond13" atomRefs="FMNH2-atom22 FMNH2-atom31" order="1"/> <bond id="FMNH2-bond14" atomRefs="FMNH2-atom20 FMNH2-atom13" order="1"/> <bond id="FMNH2-bond15" atomRefs="FMNH2-atom19 FMNH2-atom30" order="1"/> <bond id="FMNH2-bond16" atomRefs="FMNH2-atom18 FMNH2-atom10" order="1"/> <bond id="FMNH2-bond17" atomRefs="FMNH2-atom17 FMNH2-atom10" order="1"/> <bond id="FMNH2-bond18" atomRefs="FMNH2-atom16 FMNH2-atom25" order="1"/> <bond id="FMNH2-bond19" atomRefs="FMNH2-atom15 FMNH2-atom27" order="1"/> <bond id="FMNH2-bond20" atomRefs="FMNH2-atom14 FMNH2-atom11" order="1"/> <bond id="FMNH2-bond21" atomRefs="FMNH2-atom13 FMNH2-atom15" order="2"/> <bond id="FMNH2-bond22" atomRefs="FMNH2-atom12 FMNH2-atom15" order="1"/> <bond id="FMNH2-bond23" atomRefs="FMNH2-atom11 FMNH2-atom17" order="1"/> <bond id="FMNH2-bond24" atomRefs="FMNH2-atom10 FMNH2-atom16" order="1"/> <bond id="FMNH2-bond25" atomRefs="FMNH2-atom9 FMNH2-atom19" order="1"/> <bond id="FMNH2-bond26" atomRefs="FMNH2-atom8 FMNH2-atom17" order="1"/> <bond id="FMNH2-bond27" atomRefs="FMNH2-atom7 FMNH2-atom9" order="2"/> <bond id="FMNH2-bond28" atomRefs="FMNH2-atom6 FMNH2-atom13" order="1"/> <bond id="FMNH2-bond29" atomRefs="FMNH2-atom5 FMNH2-atom4" order="2"/> <bond id="FMNH2-bond30" atomRefs="FMNH2-atom4 FMNH2-atom23" order="1"/> <bond id="FMNH2-bond31" atomRefs="FMNH2-atom3 FMNH2-atom2" order="2"/> <bond id="FMNH2-bond32" atomRefs="FMNH2-atom2 FMNH2-atom21" order="1"/> <bond id="FMNH2-bond33" atomRefs="FMNH2-atom1 FMNH2-atom11" order="1"/> </bondArray> <formula concise="C 17 H 21 N 4 O 9 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">456.348</float> <string title="smiles">C1(NC(=O)NC2(N(C3(=CC(=C(C)C=C(NC1=2)3)C))CC(O)C(O)C(COP([O-])(=O)[O-])O))(=O)</string> </molecule> </cml> Reduced FMN reduced flavin mononucleotide MetaCyc FMNH2 CAS 67-63-0 LIGAND C01847 1 The enzymatic mechanism has been studied in detail |CITS: [2407239], [7978236], [7848266], [7559411], [8634296], [8703965], [8824216], [10956653], [11034781], [11784161]|. The enzyme catalyzes phosphate elimination by a 1,4-elimination mechanism that proceeds with anti-stereochemistry |CITS: [4550759]|. The <i>E. coli</i> enzyme is unable to generate reduced flavin via the oxidation of reduced nicotinamide nucleotides; it can synthesize chorismate only when supplied directly with either FMNH₂ or FADH₂, and the preferred flavin is FMNH₂ |CITS:[2969724]|. The reaction is oxygen sensitive and the enzyme is inactive under aerobic conditions |CITS:[4289188]|. The enzyme remains tetrameric and undergoes significant conformational changes during catalysis |CITS: [9761730]|. Chorismate synthase acts in the shikimate pathway. It catalyses the conversion of 5-enolpyruvylshikimate 3-phosphate into chorismate, the key branch-point intermediate in aromatic biosynthesis. Chorismate synthase is an AroC tetramer |CITS: [2969724]|. The enzymatic mechanism has been studied in detail |CITS: [2407239], [7978236], [7848266], [7559411], [8634296], [8703965], [8824216], [10956653], [11034781], [11784161]|. The enzyme catalyzes phosphate elimination by a 1,4-elimination mechanism that proceeds with anti-stereochemistry |CITS: [4550759]|. The <i>E. coli</i> enzyme is unable to generate reduced flavin via the oxidation of reduced nicotinamide nucleotides; it can synthesize chorismate only when supplied directly with either FMNH₂ or FADH₂, and the preferred flavin is FMNH₂ |CITS:[2969724]|. The reaction is oxygen sensitive and the enzyme is inactive under aerobic conditions |CITS:[4289188]|. The enzyme remains tetrameric and undergoes significant conformational changes during catalysis |CITS: [9761730]|. A 36-residue C-terminal truncation does not eliminate enzyme activity |CITS: [2182772]|. Chorismate synthase exhibits low abundance in wild-type strains |CITS:[biosoctrans8715144]|. Overproduction and purification has been described |CITS: [2969724]|. Chorismate synthase has been studied in many different organisms. Phenotypes of an <i>E. coli aroC</i> mutant are functionally complemented by production of <i>Synechocystis PCC 6803</i> AroC |CITS: [7505271]|, <i>Vibrio anguillarum</i> AroC |CITS: [8021209]|, or <i>Brucella suis</i> AroC |CITS: [11119550]|. The shikimate pathway is of great interest as a drug target |CITS: [11865437]|. <i>Salmonella typhimurium</i> AroC is required for wild-type virulence |CITS: [3058818]|, as is <i>Brucella suis</i> AroC |CITS: [11119550]|. <i>S. typhimurium</i> |CITS: [3058818], [2187747], [1311488], [7483768], [12065485], [12531654]| and <i>S. typhi</i> |CITS: [9916080], [11982332], [12065485], [12531654], [12555559]| <i>aroC</i> mutations have been used in vaccine strains. Reviews: |CITS: [8674765], [9951731], [11476485], [12521268]|. AroC Escherichia coli K-12 substr. MG1655 NCBI Taxonomy 511145 B2329 AroC MetaCyc AROC-MONOMER UniProt P12008 RefSeq NP_416832 Pfam PF01264 IN-FAMILY Swiss-Model P12008 ModBase P12008 EcoliWiki b2329 4 AROC-CPLX MetaCyc AROC-CPLX 1 IRREVERSIBLE-LEFT-TO-RIGHT chorismate synthase 5-enolpyruvylshikimate-3-phosphate phosphorylase MetaCyc CHORISMATE-SYNTHASE-ENZRXN 5-Enolpyruvoylshikimate-3-phosphate synthase catalyzes the penultimate step in chorismate biosynthesis. The synthase is activated by monovalent cations, ammonium ions being the most effective, and exhibits allosteric behavior. Glyphosate (N-phosphonomethyl glycine) acts as a competitive inhibitor with respect to PEP and as a partial uncompetitive inhibitor with respect to shikimate 3-P. |CITS: [3111378] [7744055] [7589547]| 2.5.1.19 251.109 shikimate-3-phosphate CML <cml> <molecule id="SHIKIMATE-5P" title="shikimate-3-phosphate" dictRef="dictSHIKIMATE-5P"> <atomArray> <atom id="SHIKIMATE-5P-atom1" elementType="O" x2="135500.0" y2="-96170.0" formalCharge="-1"/> <atom id="SHIKIMATE-5P-atom2" elementType="C" x2="4560.0" y2="20380.0"/> <atom id="SHIKIMATE-5P-atom3" elementType="C" x2="56360.0" y2="-47250.0"/> <atom id="SHIKIMATE-5P-atom4" elementType="C" x2="115360.0" y2="-47250.0"/> <atom id="SHIKIMATE-5P-atom5" elementType="C" x2="-94730.0" y2="20380.0"/> <atom id="SHIKIMATE-5P-atom6" elementType="C" x2="-94730.0" y2="-112960.0"/> <atom id="SHIKIMATE-5P-atom7" elementType="O" x2="-62110.0" y2="3600.0"/> <atom id="SHIKIMATE-5P-atom8" elementType="O" x2="144130.0" y2="-3120.0"/> <atom id="SHIKIMATE-5P-atom9" elementType="O" x2="-94730.0" y2="-33820.0"/> <atom id="SHIKIMATE-5P-atom10" elementType="O" x2="-94730.0" y2="-81300.0"/> <atom id="SHIKIMATE-5P-atom11" elementType="C" x2="4560.0" y2="-112960.0"/> <atom id="SHIKIMATE-5P-atom12" elementType="O" x2="-144610.0" y2="-78900.0"/> <atom id="SHIKIMATE-5P-atom13" elementType="O" x2="-62110.0" y2="-69790.0" formalCharge="-1"/> <atom id="SHIKIMATE-5P-atom14" elementType="O" x2="-26620.0" y2="-33820.0" formalCharge="-1"/> <atom id="SHIKIMATE-5P-atom15" elementType="C" x2="-144610.0" y2="-47250.0"/> <atom id="SHIKIMATE-5P-atom16" elementType="P" x2="-62110.0" y2="-33820.0"/> </atomArray> <bondArray> <bond id="SHIKIMATE-5P-bond1" atomRefs="SHIKIMATE-5P-atom16 SHIKIMATE-5P-atom9" order="1"/> <bond id="SHIKIMATE-5P-bond2" atomRefs="SHIKIMATE-5P-atom15 SHIKIMATE-5P-atom5" order="1"/> <bond id="SHIKIMATE-5P-bond3" atomRefs="SHIKIMATE-5P-atom15 SHIKIMATE-5P-atom6" order="1"/> <bond id="SHIKIMATE-5P-bond4" atomRefs="SHIKIMATE-5P-atom14 SHIKIMATE-5P-atom16" order="1"/> <bond id="SHIKIMATE-5P-bond5" atomRefs="SHIKIMATE-5P-atom13 SHIKIMATE-5P-atom16" order="1"/> <bond id="SHIKIMATE-5P-bond6" atomRefs="SHIKIMATE-5P-atom12 SHIKIMATE-5P-atom15" order="1"/> <bond id="SHIKIMATE-5P-bond7" atomRefs="SHIKIMATE-5P-atom11 SHIKIMATE-5P-atom6" order="1"/> <bond id="SHIKIMATE-5P-bond8" atomRefs="SHIKIMATE-5P-atom10 SHIKIMATE-5P-atom6" order="1"/> <bond id="SHIKIMATE-5P-bond9" atomRefs="SHIKIMATE-5P-atom9 SHIKIMATE-5P-atom5" order="1"/> <bond id="SHIKIMATE-5P-bond10" atomRefs="SHIKIMATE-5P-atom8 SHIKIMATE-5P-atom4" order="2"/> <bond id="SHIKIMATE-5P-bond11" atomRefs="SHIKIMATE-5P-atom7 SHIKIMATE-5P-atom16" order="2"/> <bond id="SHIKIMATE-5P-bond12" atomRefs="SHIKIMATE-5P-atom4 SHIKIMATE-5P-atom3" order="1"/> <bond id="SHIKIMATE-5P-bond13" atomRefs="SHIKIMATE-5P-atom3 SHIKIMATE-5P-atom2" order="2"/> <bond id="SHIKIMATE-5P-bond14" atomRefs="SHIKIMATE-5P-atom3 SHIKIMATE-5P-atom11" order="1"/> <bond id="SHIKIMATE-5P-bond15" atomRefs="SHIKIMATE-5P-atom2 SHIKIMATE-5P-atom5" order="1"/> <bond id="SHIKIMATE-5P-bond16" atomRefs="SHIKIMATE-5P-atom1 SHIKIMATE-5P-atom4" order="1"/> </bondArray> <formula concise="C 7 H 8 O 8 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">251.109</float> <string title="smiles">C([O-])(C1(CC(O)C(O)C(C=1)OP(=O)([O-])[O-]))=O</string> </molecule> </cml> shikimate-5-phosphate shikimate-5-P 3-phosphoshikimate 5-phosphoshikimate shikimate-3-P MetaCyc SHIKIMATE-5P LIGAND C03175 1 165.019 phosphoenolpyruvate CML <cml> <molecule id="PHOSPHO-ENOL-PYRUVATE" title="phosphoenolpyruvate" dictRef="dictPHOSPHO-ENOL-PYRUVATE"> <atomArray> <atom id="PHOSPHO-ENOL-PYRUVATE-atom1" elementType="O" x2="-11198.0" y2="-3071.0"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom2" elementType="O" x2="4808.0" y2="6544.0" formalCharge="-1"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom3" elementType="O" x2="-19448.0" y2="-11198.0" formalCharge="-1"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom4" elementType="C" x2="-11198.0" y2="5179.0"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom5" elementType="C" x2="-17649.0" y2="10267.0"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom6" elementType="O" x2="-2946.0" y2="-11198.0" formalCharge="-1"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom7" elementType="O" x2="-11198.0" y2="-19448.0"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom8" elementType="O" x2="-2079.0" y2="19386.0"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom9" elementType="P" x2="-11198.0" y2="-11198.0"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom10" elementType="C" x2="-2079.0" y2="11136.0"/> </atomArray> <bondArray> <bond id="PHOSPHO-ENOL-PYRUVATE-bond1" atomRefs="PHOSPHO-ENOL-PYRUVATE-atom10 PHOSPHO-ENOL-PYRUVATE-atom4" order="1"/> <bond id="PHOSPHO-ENOL-PYRUVATE-bond2" atomRefs="PHOSPHO-ENOL-PYRUVATE-atom8 PHOSPHO-ENOL-PYRUVATE-atom10" order="2"/> <bond id="PHOSPHO-ENOL-PYRUVATE-bond3" atomRefs="PHOSPHO-ENOL-PYRUVATE-atom7 PHOSPHO-ENOL-PYRUVATE-atom9" order="2"/> <bond id="PHOSPHO-ENOL-PYRUVATE-bond4" atomRefs="PHOSPHO-ENOL-PYRUVATE-atom6 PHOSPHO-ENOL-PYRUVATE-atom9" order="1"/> <bond id="PHOSPHO-ENOL-PYRUVATE-bond5" atomRefs="PHOSPHO-ENOL-PYRUVATE-atom5 PHOSPHO-ENOL-PYRUVATE-atom4" order="2"/> <bond id="PHOSPHO-ENOL-PYRUVATE-bond6" atomRefs="PHOSPHO-ENOL-PYRUVATE-atom4 PHOSPHO-ENOL-PYRUVATE-atom1" order="1"/> <bond id="PHOSPHO-ENOL-PYRUVATE-bond7" atomRefs="PHOSPHO-ENOL-PYRUVATE-atom3 PHOSPHO-ENOL-PYRUVATE-atom9" order="1"/> <bond id="PHOSPHO-ENOL-PYRUVATE-bond8" atomRefs="PHOSPHO-ENOL-PYRUVATE-atom2 PHOSPHO-ENOL-PYRUVATE-atom10" order="1"/> <bond id="PHOSPHO-ENOL-PYRUVATE-bond9" atomRefs="PHOSPHO-ENOL-PYRUVATE-atom1 PHOSPHO-ENOL-PYRUVATE-atom9" order="1"/> </bondArray> <formula concise="C 3 H 2 O 6 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">165.019</float> <string title="smiles">C=C(OP([O-])([O-])=O)C([O-])=O</string> </molecule> </cml> P-enol-pyruvate P-enol-pyr PEP MetaCyc PHOSPHO-ENOL-PYRUVATE LIGAND C00074 CAS 138-08-9 1 3-phosphoshikimate 1-carboxyvinyltransferase 1 1 5-enolpyruvylshikimate-3-phosphate synthase EPSP synthase 3-enol-pyruvoylshikimate-5-phosphate synthase MetaCyc 2.5.1.19-RXN UniProt P11043 UniProt P0A6D3 RELATED-TO UniProt P19688 UniProt P07637 UniProt P12421 UniProt Q59975 UniProt P43905 UniProt Q04570 UniProt P23281 UniProt P23981 UniProt P24497 UniProt P17688 UniProt P19786 UniProt Q03421 UniProt Q9JTT3 UniProt P52312 UniProt P22487 UniProt P08566 RELATED-TO UniProt P07547 RELATED-TO UniProt P22299 When the enzyme is exposed to ammonium ions only monomers are present. In the absence of ammonium ions both monomers and dimers are found. Both forms are catalytically active. |CITS: [7744055]| AROEBACSU-MONOMER AroE MetaCyc AROEBACSU-MONOMER 1 REVERSIBLE 5-enolpyruvoylshikimate-3-phosphate synthase EPSP synthase 3-phosphoshikimate 1-carboxyvinyltransferase 5-enolpyruvylshikimate-3-phosphate synthase phosphoenolpyruvate:3-phosphoshikimate 5-O-(1-carboxyvinyl)-transferase MetaCyc ENZRXN-1461 EPSP synthase catalyzes the transfer of the enolpyruvoyl moiety from phosphoenolpyruvate to the hydroxyl group of carbon 5 of shikimate 3-phosphate with the elimination of phosphate to produce 5-enolpyruvoyl shikimate 3-phosphate (EPSP). |CITS:[3284585]| This is an addition-elimination reaction. It is an ordered reaction in which shikimate 3-phosphate binds first. It involves the transfer of an enolpyruvyl group unchanged to the acceptor molecule. The reaction introduces the three carbon fragment that is destined to become the side chain of phenylalanine and tyrosine and to be removed again in the synthesis of tryptophan. |CITS:[ColiSalII]| Two reactive cysteines have been identified. |CITS:[JBC263-1798-88]| A lysine has been designated a potential active site residue |CITS:[3121621]| Mechanistic and steriochemical studies on EPSP synthase suggest that a phospholactyl intermediate is produced at least transiently during the enzymatic reaction by addition of a nucleophile to C-2 of P-enolpyruvate on the pathway to phosphate release. The nucleophie may be the side chain of an active site amino acid residue based on the exchange of the C-3 hydrogens of P-enolpyruvate in the presense of the substrate analog 4,5-deoxyshikimate 3-phosphate|CITS:[JBC263-1798-88]| 3-D structure has been studied |CITS:[PNAS88-5046-91]| AROA-MONOMER B0908 AroA MetaCyc AROA-MONOMER PDB 1G6S PDB 1G6T PDB 1MI4 RefSeq NP_415428 Pfam PF00275 IN-FAMILY UniProt P0A6D3 ModBase P0A6D3 EcoliWiki b0908 1 REVERSIBLE 3-phosphoshikimate-1-carboxyvinyltransferase 5-enol-pyruvylshikimate-3-phosphate synthase EPSP synthase phosphoenolpyruvate: 3-phosphoshikimate 1-carboxyvinyl transferase MetaCyc 3-P-SHIK-1-CARBOXYVINYLXFERASE-ENZRXN Huynh QK Kishore GM Bild GS PubMed 3121621 J Biol Chem 1988;263(2);735-9 5-Enolpyruvyl shikimate 3-phosphate synthase from Escherichia coli. Identification of Lys-22 as a potential active site residue. 1988 Duncan K Lewendon A Coggins JR PubMed 6229418 FEBS Lett 1984;165(1);121-7 The purification of 5-enolpyruvylshikimate 3-phosphate synthase from an overproducing strain of Escherichia coli. 1984 Duncan K Coggins JR PubMed 3518706 Biochem J 1986;234(1);49-57 The serC-aro A operon of Escherichia coli. A mixed function operon encoding enzymes from two different amino acid biosynthetic pathways. 1986 Bondinell WE Vnek J Knowles PF Sprecher M Sprinson DB PubMed 4942558 J Biol Chem 1971;246(20);6191-6 On the mechanism of 5-enolpyruvylshikimate 3-phosphate synthetase. 1971 Lewendon A Coggins JR PubMed 6351837 Biochem J 1983;213(1);187-91 Purification of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli. 1983 FEBS(84)170-59 24.305 Mg2+ CML <cml> <molecule id="MG+2" title="Mg2+" dictRef="dictMG+2"> <atomArray> <atom id="MG+2-atom1" elementType="MG" x2="-999.0" y2="-999.0" formalCharge="2"/> </atomArray> <bondArray> </bondArray> <formula concise="MG 1" formalCharge="2"/> <float title="molecularWeight" units="g/mol">24.305</float> <string title="smiles">[Mg++]</string> </molecule> </cml> magnesium Mg<SUP>+2</SUP> Mg<SUP>++</SUP> magnesium ion MetaCyc MG+2 LIGAND C00305 1 Shikimate kinase catalyzes the fifth reaction in chorismate biosynthesis. The kinase forms a complex with the bifunctional DAHP synthase-chorismate mutase enzyme. The complex may serve as a regulatory unit. |CITS: [170268] [BSUB225]| 2.7.1.71 173.145 shikimate CML <cml> <molecule id="SHIKIMATE" title="shikimate" dictRef="dictSHIKIMATE"> <atomArray> <atom id="SHIKIMATE-atom1" elementType="O" x2="17747.0" y2="-8968.0"/> <atom id="SHIKIMATE-atom2" elementType="O" x2="-17974.0" y2="3407.0"/> <atom id="SHIKIMATE-atom3" elementType="C" x2="3459.0" y2="-8968.0"/> <atom id="SHIKIMATE-atom4" elementType="C" x2="-10831.0" y2="-8968.0"/> <atom id="SHIKIMATE-atom5" elementType="C" x2="10603.0" y2="-13093.0"/> <atom id="SHIKIMATE-atom6" elementType="C" x2="3459.0" y2="-718.0"/> <atom id="SHIKIMATE-atom7" elementType="O" x2="10603.0" y2="-21342.0" formalCharge="-1"/> <atom id="SHIKIMATE-atom8" elementType="C" x2="-3686.0" y2="-13093.0"/> <atom id="SHIKIMATE-atom9" elementType="C" x2="-10831.0" y2="-718.0"/> <atom id="SHIKIMATE-atom10" elementType="O" x2="-17974.0" y2="-13093.0"/> <atom id="SHIKIMATE-atom11" elementType="O" x2="-3686.0" y2="11657.0"/> <atom id="SHIKIMATE-atom12" elementType="C" x2="-3686.0" y2="3407.0"/> </atomArray> <bondArray> <bond id="SHIKIMATE-bond1" atomRefs="SHIKIMATE-atom12 SHIKIMATE-atom9" order="1"/> <bond id="SHIKIMATE-bond2" atomRefs="SHIKIMATE-atom12 SHIKIMATE-atom6" order="1"/> <bond id="SHIKIMATE-bond3" atomRefs="SHIKIMATE-atom11 SHIKIMATE-atom12" order="1"/> <bond id="SHIKIMATE-bond4" atomRefs="SHIKIMATE-atom10 SHIKIMATE-atom4" order="1"/> <bond id="SHIKIMATE-bond5" atomRefs="SHIKIMATE-atom9 SHIKIMATE-atom4" order="1"/> <bond id="SHIKIMATE-bond6" atomRefs="SHIKIMATE-atom7 SHIKIMATE-atom5" order="1"/> <bond id="SHIKIMATE-bond7" atomRefs="SHIKIMATE-atom6 SHIKIMATE-atom3" order="2"/> <bond id="SHIKIMATE-bond8" atomRefs="SHIKIMATE-atom5 SHIKIMATE-atom3" order="1"/> <bond id="SHIKIMATE-bond9" atomRefs="SHIKIMATE-atom4 SHIKIMATE-atom8" order="1"/> <bond id="SHIKIMATE-bond10" atomRefs="SHIKIMATE-atom3 SHIKIMATE-atom8" order="1"/> <bond id="SHIKIMATE-bond11" atomRefs="SHIKIMATE-atom2 SHIKIMATE-atom9" order="1"/> <bond id="SHIKIMATE-bond12" atomRefs="SHIKIMATE-atom1 SHIKIMATE-atom5" order="2"/> </bondArray> <formula concise="C 7 H 9 O 5" formalCharge="0"/> <float title="molecularWeight" units="g/mol">173.145</float> <string title="smiles">C(=O)(C1(CC(C(O)C(O)C=1)O))[O-]</string> <string title="systematicName">1-cyclohexene-1-carboxylic acid, 3,4,5-trihydroxy-</string> </molecule> </cml> shikimic acid MetaCyc SHIKIMATE CAS 138-59-0 LIGAND C00493 1 504.16 ATP CML <cml> <molecule id="ATP" title="ATP" dictRef="dictATP"> <atomArray> <atom id="ATP-atom1" elementType="O" x2="5313.0" y2="-3305.0"/> <atom id="ATP-atom2" elementType="O" x2="7289.0" y2="-1325.0"/> <atom id="ATP-atom3" elementType="O" x2="5310.0" y2="-1664.0" formalCharge="-1"/> <atom id="ATP-atom4" elementType="C" x2="9978.0" y2="-4787.0"/> <atom id="ATP-atom5" elementType="C" x2="6745.0" y2="-3029.0"/> <atom id="ATP-atom6" elementType="N" x2="9497.0" y2="-5461.0"/> <atom id="ATP-atom7" elementType="N" x2="7988.0" y2="-3957.0"/> <atom id="ATP-atom8" elementType="O" x2="6134.0" y2="-2483.0"/> <atom id="ATP-atom9" elementType="O" x2="8184.0" y2="-3250.0"/> <atom id="ATP-atom10" elementType="C" x2="7277.0" y2="-4376.0"/> <atom id="ATP-atom11" elementType="C" x2="7988.0" y2="-5616.0"/> <atom id="ATP-atom12" elementType="C" x2="8707.0" y2="-5206.0"/> <atom id="ATP-atom13" elementType="C" x2="8707.0" y2="-4376.0"/> <atom id="ATP-atom14" elementType="C" x2="7525.0" y2="-2772.0"/> <atom id="ATP-atom15" elementType="C" x2="7774.0" y2="-1987.0"/> <atom id="ATP-atom16" elementType="C" x2="8599.0" y2="-1987.0"/> <atom id="ATP-atom17" elementType="C" x2="8852.0" y2="-2772.0"/> <atom id="ATP-atom18" elementType="N" x2="7277.0" y2="-5206.0"/> <atom id="ATP-atom19" elementType="N" x2="9495.0" y2="-4128.0"/> <atom id="ATP-atom20" elementType="P" x2="5312.0" y2="-2484.0"/> <atom id="ATP-atom21" elementType="N" x2="7985.0" y2="-6441.0"/> <atom id="ATP-atom22" elementType="O" x2="9084.0" y2="-1320.0"/> <atom id="ATP-atom23" elementType="O" x2="4492.0" y2="-2484.0"/> <atom id="ATP-atom24" elementType="O" x2="3667.0" y2="-3311.0"/> <atom id="ATP-atom25" elementType="O" x2="3664.0" y2="-1661.0" formalCharge="-1"/> <atom id="ATP-atom26" elementType="P" x2="3666.0" y2="-2486.0"/> <atom id="ATP-atom27" elementType="O" x2="2841.0" y2="-2486.0"/> <atom id="ATP-atom28" elementType="O" x2="2016.0" y2="-3313.0"/> <atom id="ATP-atom29" elementType="O" x2="2013.0" y2="-1663.0" formalCharge="-1"/> <atom id="ATP-atom30" elementType="O" x2="1190.0" y2="-2488.0"/> <atom id="ATP-atom31" elementType="P" x2="2015.0" y2="-2488.0"/> </atomArray> <bondArray> <bond id="ATP-bond1" atomRefs="ATP-atom30 ATP-atom31" order="1"/> <bond id="ATP-bond2" atomRefs="ATP-atom29 ATP-atom31" order="1"/> <bond id="ATP-bond3" atomRefs="ATP-atom28 ATP-atom31" order="2"/> <bond id="ATP-bond4" atomRefs="ATP-atom27 ATP-atom31" order="1"/> <bond id="ATP-bond5" atomRefs="ATP-atom27 ATP-atom26" order="1"/> <bond id="ATP-bond6" atomRefs="ATP-atom25 ATP-atom26" order="1"/> <bond id="ATP-bond7" atomRefs="ATP-atom24 ATP-atom26" order="2"/> <bond id="ATP-bond8" atomRefs="ATP-atom23 ATP-atom26" order="1"/> <bond id="ATP-bond9" atomRefs="ATP-atom16 ATP-atom22" order="1"/> <bond id="ATP-bond10" atomRefs="ATP-atom21 ATP-atom11" order="1"/> <bond id="ATP-bond11" atomRefs="ATP-atom1 ATP-atom20" order="2"/> <bond id="ATP-bond12" atomRefs="ATP-atom15 ATP-atom2" order="1"/> <bond id="ATP-bond13" atomRefs="ATP-atom3 ATP-atom20" order="1"/> <bond id="ATP-bond14" atomRefs="ATP-atom6 ATP-atom4" order="2"/> <bond id="ATP-bond15" atomRefs="ATP-atom4 ATP-atom19" order="1"/> <bond id="ATP-bond16" atomRefs="ATP-atom5 ATP-atom8" order="1"/> <bond id="ATP-bond17" atomRefs="ATP-atom14 ATP-atom5" order="1"/> <bond id="ATP-bond18" atomRefs="ATP-atom12 ATP-atom6" order="1"/> <bond id="ATP-bond19" atomRefs="ATP-atom10 ATP-atom7" order="2"/> <bond id="ATP-bond20" atomRefs="ATP-atom7 ATP-atom13" order="1"/> <bond id="ATP-bond21" atomRefs="ATP-atom8 ATP-atom20" order="1"/> <bond id="ATP-bond22" atomRefs="ATP-atom9 ATP-atom14" order="1"/> <bond id="ATP-bond23" atomRefs="ATP-atom9 ATP-atom17" order="1"/> <bond id="ATP-bond24" atomRefs="ATP-atom23 ATP-atom20" order="1"/> <bond id="ATP-bond25" atomRefs="ATP-atom18 ATP-atom10" order="1"/> <bond id="ATP-bond26" atomRefs="ATP-atom12 ATP-atom11" order="1"/> <bond id="ATP-bond27" atomRefs="ATP-atom11 ATP-atom18" order="2"/> <bond id="ATP-bond28" atomRefs="ATP-atom13 ATP-atom12" order="2"/> <bond id="ATP-bond29" atomRefs="ATP-atom19 ATP-atom13" order="1"/> <bond id="ATP-bond30" atomRefs="ATP-atom14 ATP-atom15" order="1"/> <bond id="ATP-bond31" atomRefs="ATP-atom15 ATP-atom16" order="1"/> <bond id="ATP-bond32" atomRefs="ATP-atom16 ATP-atom17" order="1"/> <bond id="ATP-bond33" atomRefs="ATP-atom17 ATP-atom19" order="1"/> </bondArray> <formula concise="C 10 H 13 N 5 O 13 P 3" formalCharge="-4"/> <float title="molecularWeight" units="g/mol">504.16</float> <string title="smiles">C(C3(C(C(C(N2(C1(=C(C(=NC=N1)N)N=C2)))O3)O)O))OP(OP(=O)([O-])OP(=O)([O-])O)([O-])=O</string> </molecule> </cml> adenylpyrophosphate adenosine-triphosphate adenosine-5'-triphosphate MetaCyc ATP CAS 56-65-5 LIGAND C00002 1 shikimate-kinase H+ hydrogen ion proton H MetaCyc PROTON LIGAND C00080 CAS 12408-02-5 ChEBI 24636 LIGAND C00080 PubChem 1038 2 1 424.18 ADP CML <cml> <molecule id="ADP" title="ADP" dictRef="dictADP"> <atomArray> <atom id="ADP-atom1" elementType="O" x2="5313.0" y2="-3305.0"/> <atom id="ADP-atom2" elementType="O" x2="7289.0" y2="-1325.0"/> <atom id="ADP-atom3" elementType="O" x2="5310.0" y2="-1664.0" formalCharge="-1"/> <atom id="ADP-atom4" elementType="C" x2="9978.0" y2="-4787.0"/> <atom id="ADP-atom5" elementType="C" x2="6745.0" y2="-3029.0"/> <atom id="ADP-atom6" elementType="N" x2="9497.0" y2="-5461.0"/> <atom id="ADP-atom7" elementType="N" x2="7988.0" y2="-3957.0"/> <atom id="ADP-atom8" elementType="O" x2="6134.0" y2="-2483.0"/> <atom id="ADP-atom9" elementType="O" x2="8184.0" y2="-3250.0"/> <atom id="ADP-atom10" elementType="C" x2="7277.0" y2="-4376.0"/> <atom id="ADP-atom11" elementType="C" x2="7988.0" y2="-5616.0"/> <atom id="ADP-atom12" elementType="C" x2="8707.0" y2="-5206.0"/> <atom id="ADP-atom13" elementType="C" x2="8707.0" y2="-4376.0"/> <atom id="ADP-atom14" elementType="C" x2="7525.0" y2="-2772.0"/> <atom id="ADP-atom15" elementType="C" x2="7774.0" y2="-1987.0"/> <atom id="ADP-atom16" elementType="C" x2="8599.0" y2="-1987.0"/> <atom id="ADP-atom17" elementType="C" x2="8852.0" y2="-2772.0"/> <atom id="ADP-atom18" elementType="N" x2="7277.0" y2="-5206.0"/> <atom id="ADP-atom19" elementType="N" x2="9495.0" y2="-4128.0"/> <atom id="ADP-atom20" elementType="P" x2="5312.0" y2="-2484.0"/> <atom id="ADP-atom21" elementType="N" x2="7985.0" y2="-6441.0"/> <atom id="ADP-atom22" elementType="O" x2="9084.0" y2="-1320.0"/> <atom id="ADP-atom23" elementType="O" x2="4492.0" y2="-2484.0"/> <atom id="ADP-atom24" elementType="O" x2="3667.0" y2="-3311.0"/> <atom id="ADP-atom25" elementType="O" x2="3664.0" y2="-1661.0" formalCharge="-1"/> <atom id="ADP-atom26" elementType="P" x2="3666.0" y2="-2486.0"/> <atom id="ADP-atom27" elementType="O" x2="2841.0" y2="-2486.0" formalCharge="-1"/> </atomArray> <bondArray> <bond id="ADP-bond1" atomRefs="ADP-atom27 ADP-atom26" order="1"/> <bond id="ADP-bond2" atomRefs="ADP-atom25 ADP-atom26" order="1"/> <bond id="ADP-bond3" atomRefs="ADP-atom24 ADP-atom26" order="2"/> <bond id="ADP-bond4" atomRefs="ADP-atom23 ADP-atom26" order="1"/> <bond id="ADP-bond5" atomRefs="ADP-atom16 ADP-atom22" order="1"/> <bond id="ADP-bond6" atomRefs="ADP-atom21 ADP-atom11" order="1"/> <bond id="ADP-bond7" atomRefs="ADP-atom1 ADP-atom20" order="2"/> <bond id="ADP-bond8" atomRefs="ADP-atom15 ADP-atom2" order="1"/> <bond id="ADP-bond9" atomRefs="ADP-atom3 ADP-atom20" order="1"/> <bond id="ADP-bond10" atomRefs="ADP-atom6 ADP-atom4" order="2"/> <bond id="ADP-bond11" atomRefs="ADP-atom4 ADP-atom19" order="1"/> <bond id="ADP-bond12" atomRefs="ADP-atom5 ADP-atom8" order="1"/> <bond id="ADP-bond13" atomRefs="ADP-atom14 ADP-atom5" order="1"/> <bond id="ADP-bond14" atomRefs="ADP-atom12 ADP-atom6" order="1"/> <bond id="ADP-bond15" atomRefs="ADP-atom10 ADP-atom7" order="2"/> <bond id="ADP-bond16" atomRefs="ADP-atom7 ADP-atom13" order="1"/> <bond id="ADP-bond17" atomRefs="ADP-atom8 ADP-atom20" order="1"/> <bond id="ADP-bond18" atomRefs="ADP-atom9 ADP-atom14" order="1"/> <bond id="ADP-bond19" atomRefs="ADP-atom9 ADP-atom17" order="1"/> <bond id="ADP-bond20" atomRefs="ADP-atom23 ADP-atom20" order="1"/> <bond id="ADP-bond21" atomRefs="ADP-atom18 ADP-atom10" order="1"/> <bond id="ADP-bond22" atomRefs="ADP-atom12 ADP-atom11" order="1"/> <bond id="ADP-bond23" atomRefs="ADP-atom11 ADP-atom18" order="2"/> <bond id="ADP-bond24" atomRefs="ADP-atom13 ADP-atom12" order="2"/> <bond id="ADP-bond25" atomRefs="ADP-atom19 ADP-atom13" order="1"/> <bond id="ADP-bond26" atomRefs="ADP-atom14 ADP-atom15" order="1"/> <bond id="ADP-bond27" atomRefs="ADP-atom15 ADP-atom16" order="1"/> <bond id="ADP-bond28" atomRefs="ADP-atom16 ADP-atom17" order="1"/> <bond id="ADP-bond29" atomRefs="ADP-atom17 ADP-atom19" order="1"/> </bondArray> <formula concise="C 10 H 12 N 5 O 10 P 2" formalCharge="-3"/> <float title="molecularWeight" units="g/mol">424.18</float> <string title="smiles">C(C3(C(C(C(N2(C1(=C(C(=NC=N1)N)N=C2)))O3)O)O))OP(OP(=O)([O-])[O-])([O-])=O</string> </molecule> </cml> adenosine pyrophosphate adenosine 5'-pyrophosphate adenosine-5'-diphosphate adenosine-diphosphate adenosine-5-diphosphate MetaCyc ADP CAS 58-64-0 LIGAND C00008 CAS 20398-34-9 1 MetaCyc SHIKIMATE-KINASE-RXN UniProt P72796 UniProt P43906 UniProt P34003 UniProt Q00497 UniProt P10880 UniProt P0A6E1 RELATED-TO UniProt P37944 UniProt Q9CEU1 UniProt P63600 UniProt P43880 UniProt P08566 RELATED-TO UniProt P07547 RELATED-TO UniProt Q9PIB5 UniProt P0A6D7 RELATED-TO AROIBACSU-MONOMER AroI MetaCyc AROIBACSU-MONOMER 1 REVERSIBLE shikimate kinase ATP:shikimate 3-phosphotransferase MetaCyc ENZRXN-1444 1 E. coli has two shikimate kinase enzymes, I and II. The isoenzymes are separable and presumably monofunctional. |CITS:[3026317]| There are two enzymes able to convert shikimate to shikimate 3-phosphate, step five in the biosynthesis of aromatic compounds. With the exception of shikimate kinase, the other enzymes of the common pathway are synthesized constitutively. |CITS:[3001024]| The Km for shikimate kinase II is much lower than for shikimate kinase I. |CITS: [1309529]| Presumably the strains lacking the two major DAHP synthase isoenzymes (aroF and aroG) cannot accumulate an internal pool of shikimate that is sufficient for shikimate kinase I alone to carry out the phosphorylation, but the reaction can be performed by shikimate kinase II. Studies on the affinity of the shikimate kinase isoenzymes for shikimate support this interpretation. |CITS:[3001024]| The level of shikimate kinase in coli can be repressed and derepressed. Both tyrosine and tryptophan, but not phenylalanine are apparently involved in this control. Starvation for both of these amino acids results in derepression. In a fully repressed cell, shikimate kinase I is the predominant shikimate kinase activity. However, a mutation in tyrR or the partial starvation of an aromatic auxotroph for tyrosine and tryptophan appears to alter only the level of shikimate kinase II which now becomes the cell's major shikimate kinase activity |CITS:[222728]|. In contrast to shikimate kinase II, the activity of shikimate kinase I in the cell is independent of both the amount of extracellular aromatic amino acids and the level of tyrR gene products |CITS:[1309529]|. Amino acids and biosynthetic intermediates were tested for inhibitory effects. Neither the aromatic amino acids, either singly or all together, nor a mixture of aromatic amino acids and vitamins at the concentrations used caused inhibition of either shikimate kinase I or shikimate kinase II activity. Similarly neither chorismic acid nor prephenic acid, two key biosynthetic intermediates in the aromatic pathway, had a significant effect on these shikimate kinase activities. shikimate kinase I B3390 AroK shikimic acid kinase I MetaCyc AROK-MONOMER PDB 1KAG Pfam PF01202 IN-FAMILY UniProt P0A6D7 ModBase P0A6D7 RefSeq YP_026215 EcoliWiki b3390 Lobner-Olesen A Marinus MG PubMed 1309529 J Bacteriol 1992;174(2);525-9 Identification of the gene (aroK) encoding shikimic acid kinase I of Escherichia coli. 1992 1 shikimate kinase shikimic acid kinase MetaCyc SHIKIMATE-KINASEI-ENZRXN DeFeyter RC Pittard J PubMed 3001029 J Bacteriol 1986;165(1);331-3 Purification and properties of shikimate kinase II from Escherichia coli K-12. 1986 Millar G Lewendon A Hunter MG Coggins JR PubMed 3026317 Biochem J 1986;237(2);427-37 The cloning and expression of the aroL gene from Escherichia coli K12. Purification and complete amino acid sequence of shikimate kinase II, the aroL-gene product. 1986 DeFeyter RC Davidson BE Pittard J PubMed 3001025 J Bacteriol 1986;165(1);233-9 Nucleotide sequence of the transcription unit containing the aroL and aroM genes from Escherichia coli K-12. 1986 DeFeyter RC Pittard J PubMed 3001024 J Bacteriol 1986;165(1);226-32 Genetic and molecular analysis of aroL, the gene for shikimate kinase II in Escherichia coli K-12. 1986 Ely B Pittard J PubMed 222728 J Bacteriol 1979;138(3);933-43 Aromatic amino acid biosynthesis: regulation of shikimate kinase in Escherichia coli K-12. 1979 1 E. coli has 2 shikimate kinase enzymes, I and II. The isoenzymes are separable and presumably monofunctional. There are two enzymes able to convert shikimate to shikimate 3-phosphate, step five in the biosynthesis of aromatic compounds. With the exception of shikimate kinase, the other enzymes of the common pathway are synthesized constitutively. The Km for shikimate II is much lower than for shikimate kinase I. Presumably the strains lacking the two major DAHP synthase isoenzymes (aroF and aroG) cannot accumulate an internal poll of shikmate that is sufficient for shikimate kinase I alone to carry out the phosphrylatioon but the reaction can be performed by shikimate kinase II. Studies on the affinity of the shikmate kinase isoenzymes for shikimate support this interpretation. |CITS:[3001024]|. The level of shikimate kinase in coli can be repressed and derepressed. Both tyrosine and tryptophan, but not phenylalanine are apparently involved in this control. Starvation for both of these amino acids results in derepression. In a fully represssed cell, shikimate kinase I is the predominant shikimate kinase actiity. However, a mutation in tyrR or the partial starvation of an aromatic auxotroph for tyrosine and tryptophan appears to alter only the level of shikimate kinase II which now becomes the cell's major shikimate kinase activity |CITS:[222728]|. Amino acids and biosynthetic intermediates were tested for inhibitory effects. Neither the aromatic amino acids, either singly or all together, nor a mixture of aromatic amino acids and vitamins at the concentrations used caused inhbition of either shikimate kinase I or shikimate kinase II activity. Similarly neither chorismic acid nor prephenic acid, two key biosynthetic intermediates in the aromatic pathway, had a significant effect on these shikimate kinase activities. Expression of the structural gene of one of the coli shikimate kinase isoenzyme, the aroL gene product is regulated by the tyrR gene product protein with tyrosine or tryptophan as co-repressor. |CITS:[3026317]| A second gene, designated aroM, that encodes a 26-kilodalton gene product of unknown function was shown to be cotranscribed with aroL. |CITS:[3001025]| shikimate kinase II B0388 AroL MetaCyc AROL-MONOMER RefSeq NP_414922 Pfam PF01202 IN-FAMILY UniProt P0A6E1 Swiss-Model P0A6E1 ModBase P0A6E1 EcoliWiki b0388 1 shikimate kinase MetaCyc SHIKIMATE-KINASEII-ENZRXN Shikimate 5-dehydrogenase catalyzes the fourth reaction in chorismate biosynthesis. |CITS: [BSUB225]| 1.1.1.25 1 |FRAME: NAD| and |FRAME: NADP| are two forms of |FRAME: NIACINE|. These molecules are the biological carriers of reductive equivalents (i.e. high potential electrons). They are often referred to as coenzymes, although in most of their reactions they function as cosubstrates rather than true coenzymes. The most common function of NAD+ is to accept two electrons and a proton (a hidride ion) from a substrate that is being oxidized. This reduction converts NAD+ to |FRAME: NADH|, the reduced form. NADH then diffuses or is being transported to a terminal oxidase, where the electrons are passed on, regenerating the oxidized form. |FRAME: NADPH|, on the other hand, is mostly involved in biosynthetic reactions, where it serves as an electron donor. NADPH is formed by reduction of NADP+, which occurs by different mechanisms in different types of organisms. In photosynthetic organisms NADP+ is reduced by |FRAME: CPLX-84|. In heterotrophic organisms NADP+ is reduced by central metabolism processes such as the pentose phosphate pathway (see |FRAME: OXIDATIVEPENT-PWY|). 740.386 NADP+ CML <cml> <molecule id="NADP" title="NADP+" dictRef="dictNADP"> <atomArray> <atom id="NADP-atom1" elementType="O" x2="53130.0" y2="-33049.0"/> <atom id="NADP-atom2" elementType="O" x2="72891.0" y2="-13253.0"/> <atom id="NADP-atom3" elementType="O" x2="53105.0" y2="-16639.0" formalCharge="-1"/> <atom id="NADP-atom4" elementType="C" x2="99778.0" y2="-47867.0"/> <atom id="NADP-atom5" elementType="C" x2="67454.0" y2="-30291.0"/> <atom id="NADP-atom6" elementType="N" x2="94969.0" y2="-54609.0"/> <atom id="NADP-atom7" elementType="N" x2="79875.0" y2="-39567.0"/> <atom id="NADP-atom8" elementType="O" x2="61335.0" y2="-24826.0"/> <atom id="NADP-atom9" elementType="O" x2="81839.0" y2="-32502.0"/> <atom id="NADP-atom10" elementType="C" x2="72769.0" y2="-43761.0"/> <atom id="NADP-atom11" elementType="C" x2="79875.0" y2="-56161.0"/> <atom id="NADP-atom12" elementType="C" x2="87072.0" y2="-52058.0"/> <atom id="NADP-atom13" elementType="C" x2="87072.0" y2="-43761.0"/> <atom id="NADP-atom14" elementType="C" x2="75247.0" y2="-27725.0"/> <atom id="NADP-atom15" elementType="C" x2="77737.0" y2="-19874.0"/> <atom id="NADP-atom16" elementType="C" x2="85987.0" y2="-19874.0"/> <atom id="NADP-atom17" elementType="C" x2="88524.0" y2="-27725.0"/> <atom id="NADP-atom18" elementType="N" x2="72769.0" y2="-52058.0"/> <atom id="NADP-atom19" elementType="N" x2="94949.0" y2="-41282.0"/> <atom id="NADP-atom20" elementType="P" x2="53121.0" y2="-24844.0"/> <atom id="NADP-atom21" elementType="N" x2="79852.0" y2="-64411.0"/> <atom id="NADP-atom22" elementType="O" x2="44916.0" y2="-24844.0"/> <atom id="NADP-atom23" elementType="O" x2="36666.0" y2="-33112.0"/> <atom id="NADP-atom24" elementType="O" x2="36641.0" y2="-16612.0" formalCharge="-1"/> <atom id="NADP-atom25" elementType="P" x2="36657.0" y2="-24862.0"/> <atom id="NADP-atom26" elementType="O" x2="90842.0" y2="-13204.0"/> <atom id="NADP-atom27" elementType="P" x2="99092.0" y2="-13204.0"/> <atom id="NADP-atom28" elementType="O" x2="99092.0" y2="-21454.0"/> <atom id="NADP-atom29" elementType="O" x2="107342.0" y2="-13204.0" formalCharge="-1"/> <atom id="NADP-atom30" elementType="O" x2="99092.0" y2="-4954.0" formalCharge="-1"/> <atom id="NADP-atom31" elementType="C" x2="14118.0" y2="-24811.0"/> <atom id="NADP-atom32" elementType="C" x2="769.0" y2="-24811.0"/> <atom id="NADP-atom33" elementType="C" x2="3318.0" y2="-16965.0"/> <atom id="NADP-atom34" elementType="C" x2="11568.0" y2="-16965.0"/> <atom id="NADP-atom35" elementType="O" x2="7443.0" y2="-29660.0"/> <atom id="NADP-atom36" elementType="O" x2="-1531.0" y2="-10291.0"/> <atom id="NADP-atom37" elementType="O" x2="16418.0" y2="-10291.0"/> <atom id="NADP-atom38" elementType="C" x2="-7077.0" y2="-35610.0"/> <atom id="NADP-atom39" elementType="C" x2="-14222.0" y2="-39735.0"/> <atom id="NADP-atom40" elementType="C" x2="-21367.0" y2="-35610.0"/> <atom id="NADP-atom41" elementType="C" x2="-21367.0" y2="-27360.0"/> <atom id="NADP-atom42" elementType="C" x2="-14222.0" y2="-23235.0"/> <atom id="NADP-atom43" elementType="C" x2="-28511.0" y2="-23235.0"/> <atom id="NADP-atom44" elementType="O" x2="-28511.0" y2="-14985.0"/> <atom id="NADP-atom45" elementType="N" x2="-35656.0" y2="-27360.0"/> <atom id="NADP-atom46" elementType="N" x2="-7077.0" y2="-27360.0" formalCharge="1"/> <atom id="NADP-atom47" elementType="C" x2="21248.0" y2="-28961.0"/> <atom id="NADP-atom48" elementType="O" x2="28407.0" y2="-24862.0"/> </atomArray> <bondArray> <bond id="NADP-bond1" atomRefs="NADP-atom47 NADP-atom48" order="1"/> <bond id="NADP-bond2" atomRefs="NADP-atom31 NADP-atom47" order="1"/> <bond id="NADP-bond3" atomRefs="NADP-atom43 NADP-atom45" order="1"/> <bond id="NADP-bond4" atomRefs="NADP-atom43 NADP-atom44" order="2"/> <bond id="NADP-bond5" atomRefs="NADP-atom41 NADP-atom43" order="1"/> <bond id="NADP-bond6" atomRefs="NADP-atom42 NADP-atom41" order="1"/> <bond id="NADP-bond7" atomRefs="NADP-atom41 NADP-atom40" order="2"/> <bond id="NADP-bond8" atomRefs="NADP-atom40 NADP-atom39" order="1"/> <bond id="NADP-bond9" atomRefs="NADP-atom39 NADP-atom38" order="2"/> <bond id="NADP-bond10" atomRefs="NADP-atom38 NADP-atom46" order="1"/> <bond id="NADP-bond11" atomRefs="NADP-atom46 NADP-atom42" order="2"/> <bond id="NADP-bond12" atomRefs="NADP-atom34 NADP-atom37" order="1"/> <bond id="NADP-bond13" atomRefs="NADP-atom33 NADP-atom36" order="1"/> <bond id="NADP-bond14" atomRefs="NADP-atom32 NADP-atom46" order="1"/> <bond id="NADP-bond15" atomRefs="NADP-atom33 NADP-atom34" order="1"/> <bond id="NADP-bond16" atomRefs="NADP-atom32 NADP-atom33" order="1"/> <bond id="NADP-bond17" atomRefs="NADP-atom35 NADP-atom32" order="1"/> <bond id="NADP-bond18" atomRefs="NADP-atom35 NADP-atom31" order="1"/> <bond id="NADP-bond19" atomRefs="NADP-atom34 NADP-atom31" order="1"/> <bond id="NADP-bond20" atomRefs="NADP-atom27 NADP-atom28" order="2"/> <bond id="NADP-bond21" atomRefs="NADP-atom27 NADP-atom30" order="1"/> <bond id="NADP-bond22" atomRefs="NADP-atom27 NADP-atom29" order="1"/> <bond id="NADP-bond23" atomRefs="NADP-atom26 NADP-atom27" order="1"/> <bond id="NADP-bond24" atomRefs="NADP-atom48 NADP-atom25" order="1"/> <bond id="NADP-bond25" atomRefs="NADP-atom24 NADP-atom25" order="1"/> <bond id="NADP-bond26" atomRefs="NADP-atom23 NADP-atom25" order="2"/> <bond id="NADP-bond27" atomRefs="NADP-atom22 NADP-atom25" order="1"/> <bond id="NADP-bond28" atomRefs="NADP-atom16 NADP-atom26" order="1"/> <bond id="NADP-bond29" atomRefs="NADP-atom21 NADP-atom11" order="1"/> <bond id="NADP-bond30" atomRefs="NADP-atom1 NADP-atom20" order="2"/> <bond id="NADP-bond31" atomRefs="NADP-atom15 NADP-atom2" order="1"/> <bond id="NADP-bond32" atomRefs="NADP-atom3 NADP-atom20" order="1"/> <bond id="NADP-bond33" atomRefs="NADP-atom6 NADP-atom4" order="2"/> <bond id="NADP-bond34" atomRefs="NADP-atom4 NADP-atom19" order="1"/> <bond id="NADP-bond35" atomRefs="NADP-atom5 NADP-atom8" order="1"/> <bond id="NADP-bond36" atomRefs="NADP-atom14 NADP-atom5" order="1"/> <bond id="NADP-bond37" atomRefs="NADP-atom12 NADP-atom6" order="1"/> <bond id="NADP-bond38" atomRefs="NADP-atom10 NADP-atom7" order="2"/> <bond id="NADP-bond39" atomRefs="NADP-atom7 NADP-atom13" order="1"/> <bond id="NADP-bond40" atomRefs="NADP-atom8 NADP-atom20" order="1"/> <bond id="NADP-bond41" atomRefs="NADP-atom9 NADP-atom14" order="1"/> <bond id="NADP-bond42" atomRefs="NADP-atom9 NADP-atom17" order="1"/> <bond id="NADP-bond43" atomRefs="NADP-atom22 NADP-atom20" order="1"/> <bond id="NADP-bond44" atomRefs="NADP-atom18 NADP-atom10" order="1"/> <bond id="NADP-bond45" atomRefs="NADP-atom12 NADP-atom11" order="1"/> <bond id="NADP-bond46" atomRefs="NADP-atom11 NADP-atom18" order="2"/> <bond id="NADP-bond47" atomRefs="NADP-atom13 NADP-atom12" order="2"/> <bond id="NADP-bond48" atomRefs="NADP-atom19 NADP-atom13" order="1"/> <bond id="NADP-bond49" atomRefs="NADP-atom14 NADP-atom15" order="1"/> <bond id="NADP-bond50" atomRefs="NADP-atom15 NADP-atom16" order="1"/> <bond id="NADP-bond51" atomRefs="NADP-atom16 NADP-atom17" order="1"/> <bond id="NADP-bond52" atomRefs="NADP-atom17 NADP-atom19" order="1"/> </bondArray> <formula concise="C 21 H 25 N 7 O 17 P 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">740.386</float> <string title="smiles">C(C3(C(C(C(N2(C1(=C(C(=NC=N1)N)N=C2)))O3)OP([O-])([O-])=O)O))OP(OP(=O)([O-])OCC4(C(C(C(O4)[N+]5(=CC(=CC=C5)C(=O)N))O)O))([O-])=O</string> </molecule> </cml> coenzyme II triphosphopyridine nucleotide nicotinamide adenine dinucleotide phosphate NADP-oxidized NADP-ox NADP+ TPN TPN+ TPN-ox nicotinamide adenine dinucleotide-P NADP(+) NADP MetaCyc NADP CAS 53-59-8 LIGAND C00006 ChEBI 18009 LIGAND C00006 PubChem 5886 1 Shikimate 5-dehydrogenase 1 171.129 3-dehydro-shikimate CML <cml> <molecule id="3-DEHYDRO-SHIKIMATE" title="3-dehydro-shikimate" dictRef="dict3-DEHYDRO-SHIKIMATE"> <atomArray> <atom id="3-DEHYDRO-SHIKIMATE-atom1" elementType="C" x2="68760.0" y2="-87170.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom2" elementType="O" x2="-145580.0" y2="-128420.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom3" elementType="O" x2="-2690.0" y2="-210910.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom4" elementType="O" x2="-145580.0" y2="36580.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom5" elementType="C" x2="-74140.0" y2="-87170.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom6" elementType="C" x2="68760.0" y2="-4670.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom7" elementType="O" x2="140210.0" y2="119080.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom8" elementType="O" x2="211640.0" y2="-4670.0" formalCharge="-1"/> <atom id="3-DEHYDRO-SHIKIMATE-atom9" elementType="C" x2="-2690.0" y2="36580.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom10" elementType="C" x2="-74140.0" y2="-4670.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom11" elementType="C" x2="-2690.0" y2="-128420.0"/> <atom id="3-DEHYDRO-SHIKIMATE-atom12" elementType="C" x2="140210.0" y2="36580.0"/> </atomArray> <bondArray> <bond id="3-DEHYDRO-SHIKIMATE-bond1" atomRefs="3-DEHYDRO-SHIKIMATE-atom12 3-DEHYDRO-SHIKIMATE-atom6" order="1"/> <bond id="3-DEHYDRO-SHIKIMATE-bond2" atomRefs="3-DEHYDRO-SHIKIMATE-atom11 3-DEHYDRO-SHIKIMATE-atom1" order="1"/> <bond id="3-DEHYDRO-SHIKIMATE-bond3" atomRefs="3-DEHYDRO-SHIKIMATE-atom10 3-DEHYDRO-SHIKIMATE-atom5" order="1"/> <bond id="3-DEHYDRO-SHIKIMATE-bond4" atomRefs="3-DEHYDRO-SHIKIMATE-atom10 3-DEHYDRO-SHIKIMATE-atom9" order="1"/> <bond id="3-DEHYDRO-SHIKIMATE-bond5" atomRefs="3-DEHYDRO-SHIKIMATE-atom9 3-DEHYDRO-SHIKIMATE-atom6" order="2"/> <bond id="3-DEHYDRO-SHIKIMATE-bond6" atomRefs="3-DEHYDRO-SHIKIMATE-atom8 3-DEHYDRO-SHIKIMATE-atom12" order="1"/> <bond id="3-DEHYDRO-SHIKIMATE-bond7" atomRefs="3-DEHYDRO-SHIKIMATE-atom7 3-DEHYDRO-SHIKIMATE-atom12" order="2"/> <bond id="3-DEHYDRO-SHIKIMATE-bond8" atomRefs="3-DEHYDRO-SHIKIMATE-atom6 3-DEHYDRO-SHIKIMATE-atom1" order="1"/> <bond id="3-DEHYDRO-SHIKIMATE-bond9" atomRefs="3-DEHYDRO-SHIKIMATE-atom5 3-DEHYDRO-SHIKIMATE-atom11" order="1"/> <bond id="3-DEHYDRO-SHIKIMATE-bond10" atomRefs="3-DEHYDRO-SHIKIMATE-atom4 3-DEHYDRO-SHIKIMATE-atom10" order="2"/> <bond id="3-DEHYDRO-SHIKIMATE-bond11" atomRefs="3-DEHYDRO-SHIKIMATE-atom3 3-DEHYDRO-SHIKIMATE-atom11" order="1"/> <bond id="3-DEHYDRO-SHIKIMATE-bond12" atomRefs="3-DEHYDRO-SHIKIMATE-atom2 3-DEHYDRO-SHIKIMATE-atom5" order="1"/> </bondArray> <formula concise="C 7 H 7 O 5" formalCharge="0"/> <float title="molecularWeight" units="g/mol">171.129</float> <string title="smiles">C(=O)([O-])C1(CC(O)C(O)C(=O)C=1)</string> </molecule> </cml> 3-dehydroshikimic acid 5-dehydroshikimic acid 5-dehydroshikimate MetaCyc 3-DEHYDRO-SHIKIMATE CAS 2922-42-1 LIGAND C02637 CAS 10457-99-5 1 |FRAME: NAD| and |FRAME: NADP| are two forms of |FRAME: NIACINE|. These molecules are the biological carriers of reductive equivalents (i.e. high potential electrons). They are often referred to as coenzymes, although in most of their reactions they function as cosubstrates rather than true coenzymes. The most common function of NAD+ is to accept two electrons and a proton (a hidride ion) from a substrate that is being oxidized. This reduction converts NAD+ to |FRAME: NADH|, the reduced form. NADH then diffuses or is being transported to a terminal oxidase, where the electrons are passed on, regenerating the oxidized form. |FRAME: NADPH|, on the other hand, is mostly involved in biosynthetic reactions, where it serves as an electron donor. NADPH is formed by reduction of NADP+, which occurs by different mechanisms in different types of organisms. In photosynthetic organisms NADP+ is reduced by |FRAME: CPLX-84|. In heterotrophic organisms NADP+ is reduced by central metabolism processes such as the pentose phosphate pathway (see |FRAME: OXIDATIVEPENT-PWY|). 741.394 NADPH CML <cml> <molecule id="NADPH" title="NADPH" dictRef="dictNADPH"> <atomArray> <atom id="NADPH-atom1" elementType="O" x2="53130.0" y2="-33049.0"/> <atom id="NADPH-atom2" elementType="O" x2="72891.0" y2="-13253.0"/> <atom id="NADPH-atom3" elementType="O" x2="53105.0" y2="-16639.0" formalCharge="-1"/> <atom id="NADPH-atom4" elementType="C" x2="99778.0" y2="-47867.0"/> <atom id="NADPH-atom5" elementType="C" x2="67454.0" y2="-30291.0"/> <atom id="NADPH-atom6" elementType="N" x2="94969.0" y2="-54609.0"/> <atom id="NADPH-atom7" elementType="N" x2="79875.0" y2="-39567.0"/> <atom id="NADPH-atom8" elementType="O" x2="61335.0" y2="-24826.0"/> <atom id="NADPH-atom9" elementType="O" x2="81839.0" y2="-32502.0"/> <atom id="NADPH-atom10" elementType="C" x2="72769.0" y2="-43761.0"/> <atom id="NADPH-atom11" elementType="C" x2="79875.0" y2="-56161.0"/> <atom id="NADPH-atom12" elementType="C" x2="87072.0" y2="-52058.0"/> <atom id="NADPH-atom13" elementType="C" x2="87072.0" y2="-43761.0"/> <atom id="NADPH-atom14" elementType="C" x2="75247.0" y2="-27725.0"/> <atom id="NADPH-atom15" elementType="C" x2="77737.0" y2="-19874.0"/> <atom id="NADPH-atom16" elementType="C" x2="85987.0" y2="-19874.0"/> <atom id="NADPH-atom17" elementType="C" x2="88524.0" y2="-27725.0"/> <atom id="NADPH-atom18" elementType="N" x2="72769.0" y2="-52058.0"/> <atom id="NADPH-atom19" elementType="N" x2="94949.0" y2="-41282.0"/> <atom id="NADPH-atom20" elementType="P" x2="53121.0" y2="-24844.0"/> <atom id="NADPH-atom21" elementType="N" x2="79852.0" y2="-64411.0"/> <atom id="NADPH-atom22" elementType="O" x2="44916.0" y2="-24844.0"/> <atom id="NADPH-atom23" elementType="O" x2="36666.0" y2="-33112.0"/> <atom id="NADPH-atom24" elementType="O" x2="36641.0" y2="-16612.0" formalCharge="-1"/> <atom id="NADPH-atom25" elementType="P" x2="36657.0" y2="-24862.0"/> <atom id="NADPH-atom26" elementType="O" x2="90842.0" y2="-13204.0"/> <atom id="NADPH-atom27" elementType="P" x2="99092.0" y2="-13204.0"/> <atom id="NADPH-atom28" elementType="O" x2="99092.0" y2="-21454.0"/> <atom id="NADPH-atom29" elementType="O" x2="107342.0" y2="-13204.0" formalCharge="-1"/> <atom id="NADPH-atom30" elementType="O" x2="99092.0" y2="-4954.0" formalCharge="-1"/> <atom id="NADPH-atom31" elementType="C" x2="14118.0" y2="-24811.0"/> <atom id="NADPH-atom32" elementType="C" x2="769.0" y2="-24811.0"/> <atom id="NADPH-atom33" elementType="C" x2="3318.0" y2="-16965.0"/> <atom id="NADPH-atom34" elementType="C" x2="11568.0" y2="-16965.0"/> <atom id="NADPH-atom35" elementType="O" x2="7443.0" y2="-29660.0"/> <atom id="NADPH-atom36" elementType="O" x2="-1531.0" y2="-10291.0"/> <atom id="NADPH-atom37" elementType="O" x2="16418.0" y2="-10291.0"/> <atom id="NADPH-atom38" elementType="C" x2="-7077.0" y2="-35610.0"/> <atom id="NADPH-atom39" elementType="C" x2="-14222.0" y2="-39735.0"/> <atom id="NADPH-atom40" elementType="C" x2="-21367.0" y2="-35610.0"/> <atom id="NADPH-atom41" elementType="C" x2="-21367.0" y2="-27360.0"/> <atom id="NADPH-atom42" elementType="C" x2="-14222.0" y2="-23235.0"/> <atom id="NADPH-atom43" elementType="C" x2="-28511.0" y2="-23235.0"/> <atom id="NADPH-atom44" elementType="O" x2="-28511.0" y2="-14985.0"/> <atom id="NADPH-atom45" elementType="N" x2="-35656.0" y2="-27360.0"/> <atom id="NADPH-atom46" elementType="N" x2="-7077.0" y2="-27360.0"/> <atom id="NADPH-atom47" elementType="C" x2="21248.0" y2="-28961.0"/> <atom id="NADPH-atom48" elementType="O" x2="28407.0" y2="-24862.0"/> </atomArray> <bondArray> <bond id="NADPH-bond1" atomRefs="NADPH-atom47 NADPH-atom48" order="1"/> <bond id="NADPH-bond2" atomRefs="NADPH-atom31 NADPH-atom47" order="1"/> <bond id="NADPH-bond3" atomRefs="NADPH-atom43 NADPH-atom45" order="1"/> <bond id="NADPH-bond4" atomRefs="NADPH-atom43 NADPH-atom44" order="2"/> <bond id="NADPH-bond5" atomRefs="NADPH-atom41 NADPH-atom43" order="1"/> <bond id="NADPH-bond6" atomRefs="NADPH-atom41 NADPH-atom42" order="2"/> <bond id="NADPH-bond7" atomRefs="NADPH-atom40 NADPH-atom41" order="1"/> <bond id="NADPH-bond8" atomRefs="NADPH-atom39 NADPH-atom40" order="1"/> <bond id="NADPH-bond9" atomRefs="NADPH-atom38 NADPH-atom39" order="2"/> <bond id="NADPH-bond10" atomRefs="NADPH-atom38 NADPH-atom46" order="1"/> <bond id="NADPH-bond11" atomRefs="NADPH-atom42 NADPH-atom46" order="1"/> <bond id="NADPH-bond12" atomRefs="NADPH-atom34 NADPH-atom37" order="1"/> <bond id="NADPH-bond13" atomRefs="NADPH-atom33 NADPH-atom36" order="1"/> <bond id="NADPH-bond14" atomRefs="NADPH-atom32 NADPH-atom46" order="1"/> <bond id="NADPH-bond15" atomRefs="NADPH-atom33 NADPH-atom34" order="1"/> <bond id="NADPH-bond16" atomRefs="NADPH-atom32 NADPH-atom33" order="1"/> <bond id="NADPH-bond17" atomRefs="NADPH-atom35 NADPH-atom32" order="1"/> <bond id="NADPH-bond18" atomRefs="NADPH-atom35 NADPH-atom31" order="1"/> <bond id="NADPH-bond19" atomRefs="NADPH-atom34 NADPH-atom31" order="1"/> <bond id="NADPH-bond20" atomRefs="NADPH-atom27 NADPH-atom28" order="2"/> <bond id="NADPH-bond21" atomRefs="NADPH-atom27 NADPH-atom30" order="1"/> <bond id="NADPH-bond22" atomRefs="NADPH-atom27 NADPH-atom29" order="1"/> <bond id="NADPH-bond23" atomRefs="NADPH-atom26 NADPH-atom27" order="1"/> <bond id="NADPH-bond24" atomRefs="NADPH-atom48 NADPH-atom25" order="1"/> <bond id="NADPH-bond25" atomRefs="NADPH-atom24 NADPH-atom25" order="1"/> <bond id="NADPH-bond26" atomRefs="NADPH-atom23 NADPH-atom25" order="2"/> <bond id="NADPH-bond27" atomRefs="NADPH-atom22 NADPH-atom25" order="1"/> <bond id="NADPH-bond28" atomRefs="NADPH-atom16 NADPH-atom26" order="1"/> <bond id="NADPH-bond29" atomRefs="NADPH-atom21 NADPH-atom11" order="1"/> <bond id="NADPH-bond30" atomRefs="NADPH-atom1 NADPH-atom20" order="2"/> <bond id="NADPH-bond31" atomRefs="NADPH-atom15 NADPH-atom2" order="1"/> <bond id="NADPH-bond32" atomRefs="NADPH-atom3 NADPH-atom20" order="1"/> <bond id="NADPH-bond33" atomRefs="NADPH-atom6 NADPH-atom4" order="2"/> <bond id="NADPH-bond34" atomRefs="NADPH-atom4 NADPH-atom19" order="1"/> <bond id="NADPH-bond35" atomRefs="NADPH-atom5 NADPH-atom8" order="1"/> <bond id="NADPH-bond36" atomRefs="NADPH-atom14 NADPH-atom5" order="1"/> <bond id="NADPH-bond37" atomRefs="NADPH-atom12 NADPH-atom6" order="1"/> <bond id="NADPH-bond38" atomRefs="NADPH-atom10 NADPH-atom7" order="2"/> <bond id="NADPH-bond39" atomRefs="NADPH-atom7 NADPH-atom13" order="1"/> <bond id="NADPH-bond40" atomRefs="NADPH-atom8 NADPH-atom20" order="1"/> <bond id="NADPH-bond41" atomRefs="NADPH-atom9 NADPH-atom14" order="1"/> <bond id="NADPH-bond42" atomRefs="NADPH-atom9 NADPH-atom17" order="1"/> <bond id="NADPH-bond43" atomRefs="NADPH-atom22 NADPH-atom20" order="1"/> <bond id="NADPH-bond44" atomRefs="NADPH-atom18 NADPH-atom10" order="1"/> <bond id="NADPH-bond45" atomRefs="NADPH-atom12 NADPH-atom11" order="1"/> <bond id="NADPH-bond46" atomRefs="NADPH-atom11 NADPH-atom18" order="2"/> <bond id="NADPH-bond47" atomRefs="NADPH-atom13 NADPH-atom12" order="2"/> <bond id="NADPH-bond48" atomRefs="NADPH-atom19 NADPH-atom13" order="1"/> <bond id="NADPH-bond49" atomRefs="NADPH-atom14 NADPH-atom15" order="1"/> <bond id="NADPH-bond50" atomRefs="NADPH-atom15 NADPH-atom16" order="1"/> <bond id="NADPH-bond51" atomRefs="NADPH-atom16 NADPH-atom17" order="1"/> <bond id="NADPH-bond52" atomRefs="NADPH-atom17 NADPH-atom19" order="1"/> </bondArray> <formula concise="C 21 H 26 N 7 O 17 P 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">741.394</float> <string title="smiles">C(C3(C(C(C(N2(C1(=C(C(=NC=N1)N)N=C2)))O3)OP([O-])([O-])=O)O))OP(OP(=O)([O-])OCC4(C(C(C(O4)N5(C=C(CC=C5)C(=O)N))O)O))([O-])=O</string> </molecule> </cml> Nicotinamide adenine dinucleotide phosphate - reduced NADPH+H+ NADPH2 NADPH<SUB>2</SUB> dihydrotriphosphopyridine nucleotide dihydrotriphosphopyridine nucleotide reduced dihydronicotinamide adenine dinucleotide phosphate dihydronicotinamide adenine dinucleotide phosphate reduced NADP-reduced NADP-red NADPH<SUP>+</SUP>H<SUP>+</SUP> TPNH dihydronicotinamide adenine dinucleotide-P NADP(H) MetaCyc NADPH LIGAND C00005 CAS 2646-71-1 ChEBI 16474 LIGAND C00005 PubChem 5884 1 5-dehydroshikimate reductase MetaCyc SHIKIMATE-5-DEHYDROGENASE-RXN UniProt O65917 RELATED-TO UniProt Q42947 RELATED-TO UniProt P15770 RELATED-TO UniProt Q44612 UniProt Q44611 UniProt Q44610 UniProt Q44609 UniProt Q44608 UniProt Q44606 UniProt Q9CES7 UniProt P0A6D5 RELATED-TO UniProt Q9PIA0 UniProt Q58484 UniProt P08566 RELATED-TO UniProt P07547 RELATED-TO ARODBACSU-MONOMER AroD MetaCyc ARODBACSU-MONOMER 1 REVERSIBLE shikimate 5-dehydrogenase shikimate dehydrogenase shikimate:NADP+ 5-oxidoreductase MetaCyc ENZRXN-1443 This enzyme catalyses the NADPH linked reduction of 3-dehydro-shikimate. The enzyme transfers hydrogen stereospecifically from the A-side of NADPH.|CITS:[4155957]| AROE-MONOMER B3281 AroE MetaCyc AROE-MONOMER UniProt P15770 RefSeq NP_417740 PDB 1NYT PDB 1VI2 Structure Pfam PF01488 IN-FAMILY ModBase P15770 EcoliWiki b3281 Anton IA Coggins JR PubMed 3277621 Biochem J 1988;249(2);319-26 Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. 1988 Chaudhuri S Coggins JR PubMed 3883995 Biochem J 1985;226(1);217-23 The purification of shikimate dehydrogenase from Escherichia coli. 1985 1 REVERSIBLE shikimate dehydrogenase shikimate-5-dehydrogenase dehydroshikimate reductase shikimate:NADP+ oxidoreductase NADPH-dehydroshikimate reductase MetaCyc SHIKIMATE-5-DEHYDROGENASE-ENZRXN 3-Dehydroquinate dehydratase catalyzes the third reaction in the chorismate biosynthetic pathway. |CITS: [BSUB225] [6442253]| 4.2.1.10 189.144 3-dehydroquinate CML <cml> <molecule id="DEHYDROQUINATE" title="3-dehydroquinate" dictRef="dictDEHYDROQUINATE"> <atomArray> <atom id="DEHYDROQUINATE-atom1" elementType="C" x2="9998.0" y2="-8470.0"/> <atom id="DEHYDROQUINATE-atom2" elementType="C" x2="2853.0" y2="-4345.0"/> <atom id="DEHYDROQUINATE-atom3" elementType="C" x2="2853.0" y2="3905.0"/> <atom id="DEHYDROQUINATE-atom4" elementType="C" x2="9998.0" y2="8030.0"/> <atom id="DEHYDROQUINATE-atom5" elementType="C" x2="17142.0" y2="3905.0"/> <atom id="DEHYDROQUINATE-atom6" elementType="C" x2="17142.0" y2="-4345.0"/> <atom id="DEHYDROQUINATE-atom7" elementType="O" x2="9998.0" y2="16280.0"/> <atom id="DEHYDROQUINATE-atom8" elementType="O" x2="4164.0" y2="-14304.0"/> <atom id="DEHYDROQUINATE-atom9" elementType="C" x2="15831.0" y2="-14304.0"/> <atom id="DEHYDROQUINATE-atom10" elementType="O" x2="9998.0" y2="-20137.0"/> <atom id="DEHYDROQUINATE-atom11" elementType="O" x2="24081.0" y2="-14304.0" formalCharge="-1"/> <atom id="DEHYDROQUINATE-atom12" elementType="O" x2="24287.0" y2="8030.0"/> <atom id="DEHYDROQUINATE-atom13" elementType="O" x2="-4292.0" y2="8030.0"/> </atomArray> <bondArray> <bond id="DEHYDROQUINATE-bond1" atomRefs="DEHYDROQUINATE-atom1 DEHYDROQUINATE-atom2" order="1"/> <bond id="DEHYDROQUINATE-bond2" atomRefs="DEHYDROQUINATE-atom2 DEHYDROQUINATE-atom3" order="1"/> <bond id="DEHYDROQUINATE-bond3" atomRefs="DEHYDROQUINATE-atom3 DEHYDROQUINATE-atom4" order="1"/> <bond id="DEHYDROQUINATE-bond4" atomRefs="DEHYDROQUINATE-atom4 DEHYDROQUINATE-atom5" order="1"/> <bond id="DEHYDROQUINATE-bond5" atomRefs="DEHYDROQUINATE-atom5 DEHYDROQUINATE-atom6" order="1"/> <bond id="DEHYDROQUINATE-bond6" atomRefs="DEHYDROQUINATE-atom1 DEHYDROQUINATE-atom6" order="1"/> <bond id="DEHYDROQUINATE-bond7" atomRefs="DEHYDROQUINATE-atom4 DEHYDROQUINATE-atom7" order="1"/> <bond id="DEHYDROQUINATE-bond8" atomRefs="DEHYDROQUINATE-atom1 DEHYDROQUINATE-atom8" order="1"/> <bond id="DEHYDROQUINATE-bond9" atomRefs="DEHYDROQUINATE-atom1 DEHYDROQUINATE-atom9" order="1"/> <bond id="DEHYDROQUINATE-bond10" atomRefs="DEHYDROQUINATE-atom9 DEHYDROQUINATE-atom10" order="2"/> <bond id="DEHYDROQUINATE-bond11" atomRefs="DEHYDROQUINATE-atom9 DEHYDROQUINATE-atom11" order="1"/> <bond id="DEHYDROQUINATE-bond12" atomRefs="DEHYDROQUINATE-atom5 DEHYDROQUINATE-atom12" order="1"/> <bond id="DEHYDROQUINATE-bond13" atomRefs="DEHYDROQUINATE-atom3 DEHYDROQUINATE-atom13" order="2"/> </bondArray> <formula concise="C 7 H 9 O 6" formalCharge="0"/> <float title="molecularWeight" units="g/mol">189.144</float> <string title="smiles">C([O-])(=O)C1(O)(CC(O)C(O)C(=O)C1)</string> </molecule> </cml> 3-dehydroquinic acid 5-dehydroquinic acid 5-dehydroquinate 5-de-H-quinate MetaCyc DEHYDROQUINATE CAS 10534-44-8 LIGAND C00944 1 3-dehydroquinate dehydratase 18.015 H2O CML <cml> <molecule id="WATER" title="H2O" dictRef="dictWATER"> <atomArray> <atom id="WATER-atom1" elementType="O" x2="562.0" y2="-1312.0"/> </atomArray> <bondArray> </bondArray> <formula concise="H 2 O 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">18.015</float> <string title="smiles">O</string> </molecule> </cml> H20 hydrogen oxide water MetaCyc WATER CAS 7732-18-5 LIGAND C00001 ChEBI 15377 LIGAND C00001 PubChem 962 1 1 MetaCyc 3-DEHYDROQUINATE-DEHYDRATASE-RXN UniProt O65917 RELATED-TO UniProt P73367 UniProt Q48255 UniProt Q42947 RELATED-TO UniProt P35146 UniProt P24670 UniProt P05147 UniProt Q9PJ53 UniProt P0A4Z6 UniProt Q58849 UniProt P05194 RELATED-TO UniProt P43878 UniProt P08566 RELATED-TO UniProt P07547 RELATED-TO UniProt Q9CF39 UniProt P46380 UniProt P05195 AroC AroC MetaCyc AROCBACSU-MONOMER 2 CPLX-1121 MetaCyc CPLX-1121 1 REVERSIBLE 3-dehydroquinate dehydratase DHQ dehydratase 3-dehydroquinase 3-dehydroquinate hydro-lyase MetaCyc ENZRXN-1442 This thermolabile enzyme from <i>Acinetobacter calcoaceticus</i> was assayed in crude extracts of cells induced with protocatechuate |CITS: [7592351]|. The subunit composition of this enzyme from <i>Acinetobacter calcoaceticus</i> has not been reported. MONOMER-33 Acinetobacter sp. ADP1 NCBI Taxonomy 62977 QuiB catabolic 3-dehydroquinate dehydratase 3-dehydroquinase MetaCyc MONOMER-33 UniProt Q59087 Swiss-Model Q59087 ModBase Q59087 1 dehydroquinate dehydratase MetaCyc ENZRXN-35 Dehydroquinate dehydratase was partially purified from the cytoplasmic fraction of <i>Gluconobacter oxydans</i> |CITS: [14586099]|. MONOMER-0 Gluconobacter oxydans NCBI Taxonomy 442 MetaCyc MONOMER-0 1 dehydroquinate dehydratase MetaCyc ENZRXN-02 The enzyme is mechanistically and structurally very similar to the biosynthetic 3-dehydroquinase component of the arom multifunctional enzyme of N. crassa. It is known that the mechanism of the reaction catalyzed by the enzyme involves a covalent interaction between the substrate 3-dehydroquinate and a lysine residue, but the precise location of this lysine residue and the histidine residue, also implicated in the active site, remains to be established |CITS:[3541912]| The first step of the 3-dehydroquinase reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the e-amino group of a lysine at the active site of the enzyme. In addition to the lysine side chain involved in imine formation, the enzyme also requires a basic group for proton abstraction. The pH activity studies, demonstrate that both the coli and N. crassa 3-dehydroquinases require groups with pKa values near to 6, in a deprotonated from, for maximal activity. Experiments with diethylpyrocarbonate provide evidence that for both enzymes this group is the imidazole side chain of a histidine residue. |CITS:[2950851]| The reaction exhibits cis stereochemistry in both directions. Comparisons of the coli 3-dehydroquinase sequence and with the partial sequence of arom gene of aspergillus nidulans, which is known to include the 3-dehydroquinase domain, reveals significant homologies. AroD B1693 AroD MetaCyc AROD-MONOMER UniProt P05194 RefSeq NP_416208 Pfam PF01487 IN-FAMILY Swiss-Model P05194 ModBase P05194 EcoliWiki b1693 2 AROD-CPLX MetaCyc AROD-CPLX Kinghorn JR Schweizer M Giles NH Kushner SR PubMed 7021325 Gene NIL;14(1-2);73-80 The cloning and analysis of the aroD gene of E. coli K-12. 1 REVERSIBLE 3-dehydroquinate dehydratase 3-dehydroquinase DHQ dehydratase MetaCyc 3-DEHYDROQUINATE-DEHYDRATASE-ENZRXN Duncan K Chaudhuri S Campbell MS Coggins JR PubMed 3541912 Biochem J 1986;238(2);475-83 The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase. 1986 54.938 Mn2+ CML <cml> <molecule id="MN+2" title="Mn2+" dictRef="dictMN+2"> <atomArray> <atom id="MN+2-atom1" elementType="MN" x2="-999.0" y2="-701.0" formalCharge="2"/> </atomArray> <bondArray> </bondArray> <formula concise="MN 1" formalCharge="2"/> <float title="molecularWeight" units="g/mol">54.938</float> <string title="smiles">[Mn++]</string> </molecule> </cml> manganese ion Mn(II) Mn<SUP>+2</SUP> Mn<SUP>++</SUP> manganese (II) ion MetaCyc MN+2 CAS 7439-96-5 LIGAND C00034 CCO-CYTOSOL GO GO:0005829 1 |FRAME: NAD| and |FRAME: NADP| are two forms of |FRAME: NIACINE|. These molecules are the biological carriers of reductive equivalents (i.e. high potential electrons). They are often referred to as coenzymes, although in most of their reactions they function as cosubstrates rather than true coenzymes. The most common function of NAD+ is to accept two electrons and a proton (a hidride ion) from a substrate that is being oxidized. This reduction converts NAD+ to |FRAME: NADH|, the reduced form. NADH then diffuses or is being transported to a terminal oxidase, where the electrons are passed on, regenerating the oxidized form. |FRAME: NADPH|, on the other hand, is mostly involved in biosynthetic reactions, where it serves as an electron donor. NADPH is formed by reduction of NADP+, which occurs by different mechanisms in different types of organisms. In photosynthetic organisms NADP+ is reduced by |FRAME: CPLX-84|. In heterotrophic organisms NADP+ is reduced by central metabolism processes such as the pentose phosphate pathway (see |FRAME: OXIDATIVEPENT-PWY|). 662.422 NAD+ CML <cml> <molecule id="NAD" title="NAD+" dictRef="dictNAD"> <atomArray> <atom id="NAD-atom1" elementType="N" x2="0.0" y2="-17074.0"/> <atom id="NAD-atom2" elementType="N" x2="115524.0" y2="-54130.0"/> <atom id="NAD-atom3" elementType="O" x2="7143.0" y2="-4696.0"/> <atom id="NAD-atom4" elementType="O" x2="88800.0" y2="-22764.0"/> <atom id="NAD-atom5" elementType="O" x2="72335.0" y2="-22824.0"/> <atom id="NAD-atom6" elementType="O" x2="108566.0" y2="-2961.0"/> <atom id="NAD-atom7" elementType="O" x2="52084.0" y2="0.0"/> <atom id="NAD-atom8" elementType="O" x2="126520.0" y2="-2914.0"/> <atom id="NAD-atom9" elementType="O" x2="34131.0" y2="0.0"/> <atom id="NAD-atom10" elementType="O" x2="88776.0" y2="-6348.0" formalCharge="-1"/> <atom id="NAD-atom11" elementType="O" x2="72306.0" y2="-6324.0" formalCharge="-1"/> <atom id="NAD-atom12" elementType="C" x2="21436.0" y2="-29446.0"/> <atom id="NAD-atom13" elementType="C" x2="14292.0" y2="-25324.0"/> <atom id="NAD-atom14" elementType="C" x2="108440.0" y2="-33473.0"/> <atom id="NAD-atom15" elementType="C" x2="28585.0" y2="-25324.0"/> <atom id="NAD-atom16" elementType="C" x2="135458.0" y2="-37583.0"/> <atom id="NAD-atom17" elementType="C" x2="21436.0" y2="-12946.0"/> <atom id="NAD-atom18" elementType="C" x2="103128.0" y2="-20006.0"/> <atom id="NAD-atom19" elementType="C" x2="56912.0" y2="-18672.0"/> <atom id="NAD-atom20" elementType="N" x2="108440.0" y2="-41770.0"/> <atom id="NAD-atom21" elementType="N" x2="115548.0" y2="-29279.0"/> <atom id="NAD-atom22" elementType="N" x2="130648.0" y2="-44325.0"/> <atom id="NAD-atom23" elementType="O" x2="97008.0" y2="-14538.0"/> <atom id="NAD-atom24" elementType="O" x2="64074.0" y2="-14574.0"/> <atom id="NAD-atom25" elementType="O" x2="117510.0" y2="-22213.0"/> <atom id="NAD-atom26" elementType="O" x2="43105.0" y2="-19372.0"/> <atom id="NAD-atom27" elementType="O" x2="80585.0" y2="-14556.0"/> <atom id="NAD-atom28" elementType="C" x2="7143.0" y2="-12946.0"/> <atom id="NAD-atom29" elementType="C" x2="115548.0" y2="-45874.0"/> <atom id="NAD-atom30" elementType="C" x2="14292.0" y2="-17074.0"/> <atom id="NAD-atom31" elementType="C" x2="122745.0" y2="-41770.0"/> <atom id="NAD-atom32" elementType="C" x2="122745.0" y2="-33473.0"/> <atom id="NAD-atom33" elementType="C" x2="113412.0" y2="-9584.0"/> <atom id="NAD-atom34" elementType="C" x2="47233.0" y2="-6677.0"/> <atom id="NAD-atom35" elementType="C" x2="121662.0" y2="-9584.0"/> <atom id="NAD-atom36" elementType="C" x2="38983.0" y2="-6677.0"/> <atom id="NAD-atom37" elementType="C" x2="110917.0" y2="-17439.0"/> <atom id="NAD-atom38" elementType="C" x2="49781.0" y2="-14520.0"/> <atom id="NAD-atom39" elementType="C" x2="124199.0" y2="-17439.0"/> <atom id="NAD-atom40" elementType="C" x2="36428.0" y2="-14520.0"/> <atom id="NAD-atom41" elementType="N" x2="130624.0" y2="-30996.0"/> <atom id="NAD-atom42" elementType="N" x2="28585.0" y2="-17074.0" formalCharge="1"/> <atom id="NAD-atom43" elementType="P" x2="88794.0" y2="-14556.0"/> <atom id="NAD-atom44" elementType="P" x2="72324.0" y2="-14574.0"/> </atomArray> <bondArray> <bond id="NAD-bond1" atomRefs="NAD-atom40 NAD-atom42" order="1"/> <bond id="NAD-bond2" atomRefs="NAD-atom39 NAD-atom41" order="1"/> <bond id="NAD-bond3" atomRefs="NAD-atom36 NAD-atom40" order="1"/> <bond id="NAD-bond4" atomRefs="NAD-atom35 NAD-atom39" order="1"/> <bond id="NAD-bond5" atomRefs="NAD-atom34 NAD-atom38" order="1"/> <bond id="NAD-bond6" atomRefs="NAD-atom34 NAD-atom36" order="1"/> <bond id="NAD-bond7" atomRefs="NAD-atom33 NAD-atom37" order="1"/> <bond id="NAD-bond8" atomRefs="NAD-atom33 NAD-atom35" order="1"/> <bond id="NAD-bond9" atomRefs="NAD-atom41 NAD-atom32" order="1"/> <bond id="NAD-bond10" atomRefs="NAD-atom32 NAD-atom31" order="2"/> <bond id="NAD-bond11" atomRefs="NAD-atom31 NAD-atom29" order="1"/> <bond id="NAD-bond12" atomRefs="NAD-atom28 NAD-atom30" order="1"/> <bond id="NAD-bond13" atomRefs="NAD-atom27 NAD-atom44" order="1"/> <bond id="NAD-bond14" atomRefs="NAD-atom27 NAD-atom43" order="1"/> <bond id="NAD-bond15" atomRefs="NAD-atom26 NAD-atom40" order="1"/> <bond id="NAD-bond16" atomRefs="NAD-atom26 NAD-atom38" order="1"/> <bond id="NAD-bond17" atomRefs="NAD-atom25 NAD-atom39" order="1"/> <bond id="NAD-bond18" atomRefs="NAD-atom25 NAD-atom37" order="1"/> <bond id="NAD-bond19" atomRefs="NAD-atom24 NAD-atom44" order="1"/> <bond id="NAD-bond20" atomRefs="NAD-atom23 NAD-atom43" order="1"/> <bond id="NAD-bond21" atomRefs="NAD-atom31 NAD-atom22" order="1"/> <bond id="NAD-bond22" atomRefs="NAD-atom21 NAD-atom32" order="1"/> <bond id="NAD-bond23" atomRefs="NAD-atom29 NAD-atom20" order="2"/> <bond id="NAD-bond24" atomRefs="NAD-atom38 NAD-atom19" order="1"/> <bond id="NAD-bond25" atomRefs="NAD-atom19 NAD-atom24" order="1"/> <bond id="NAD-bond26" atomRefs="NAD-atom37 NAD-atom18" order="1"/> <bond id="NAD-bond27" atomRefs="NAD-atom18 NAD-atom23" order="1"/> <bond id="NAD-bond28" atomRefs="NAD-atom17 NAD-atom42" order="2"/> <bond id="NAD-bond29" atomRefs="NAD-atom30 NAD-atom17" order="1"/> <bond id="NAD-bond30" atomRefs="NAD-atom16 NAD-atom41" order="1"/> <bond id="NAD-bond31" atomRefs="NAD-atom22 NAD-atom16" order="2"/> <bond id="NAD-bond32" atomRefs="NAD-atom42 NAD-atom15" order="1"/> <bond id="NAD-bond33" atomRefs="NAD-atom14 NAD-atom21" order="2"/> <bond id="NAD-bond34" atomRefs="NAD-atom20 NAD-atom14" order="1"/> <bond id="NAD-bond35" atomRefs="NAD-atom13 NAD-atom30" order="2"/> <bond id="NAD-bond36" atomRefs="NAD-atom15 NAD-atom12" order="2"/> <bond id="NAD-bond37" atomRefs="NAD-atom12 NAD-atom13" order="1"/> <bond id="NAD-bond38" atomRefs="NAD-atom11 NAD-atom44" order="1"/> <bond id="NAD-bond39" atomRefs="NAD-atom10 NAD-atom43" order="1"/> <bond id="NAD-bond40" atomRefs="NAD-atom36 NAD-atom9" order="1"/> <bond id="NAD-bond41" atomRefs="NAD-atom35 NAD-atom8" order="1"/> <bond id="NAD-bond42" atomRefs="NAD-atom34 NAD-atom7" order="1"/> <bond id="NAD-bond43" atomRefs="NAD-atom33 NAD-atom6" order="1"/> <bond id="NAD-bond44" atomRefs="NAD-atom5 NAD-atom44" order="2"/> <bond id="NAD-bond45" atomRefs="NAD-atom4 NAD-atom43" order="2"/> <bond id="NAD-bond46" atomRefs="NAD-atom3 NAD-atom28" order="2"/> <bond id="NAD-bond47" atomRefs="NAD-atom2 NAD-atom29" order="1"/> <bond id="NAD-bond48" atomRefs="NAD-atom1 NAD-atom28" order="1"/> </bondArray> <formula concise="C 21 H 26 N 7 O 14 P 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">662.422</float> <string title="smiles">C1(=CC=C(C=[N+]1C5(OC(COP(=O)([O-])OP(=O)([O-])OCC2(OC(C(O)C(O)2)N4(C=NC3(C(N)=NC=NC=34))))C(O)C(O)5))C(N)=O)</string> </molecule> </cml> beta-nicotinamide adenine dinucleotide coenzyme I diphosphopyridine nucleotide diphosphopyridine nucleotide oxidized nicotinamide adenine dinucleotide nicotinamide adenine dinucleotide oxidized NAD-oxidized NAD-ox NAD+ DPN+ DPN-ox DPN &beta;-nicotinamide adenine dinucleotide NAD MetaCyc NAD CAS 53-84-9 LIGAND C00003 1 3-Dehydroquinate synthase catalyzes the second reaction in chorismate biosynthesis. The enzyme is found in association with chorismate synthase and NADPH-dependent flavin reductase. The presence of chorismate synthase is essential for DHQ synthase activity, the flavin reductase is not. The enzyme requires a divalent metal ion; either Mn<SUP>2+</SUP> or Co<SUP>2+</SUP> will serve. NAD is also required for enzyme activity. |CITS: [97286]| 4.2.3.4 285.124 3-deoxy-D-arabino-heptulosonate-7-phosphate CML <cml> <molecule id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P" title="3-deoxy-D-arabino-heptulosonate-7-phosphate" dictRef="dict3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P"> <atomArray> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom1" elementType="O" x2="-165000.0" y2="163920.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom2" elementType="C" x2="-245330.0" y2="-83590.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom3" elementType="O" x2="-5430.0" y2="-247510.0" formalCharge="-1"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom4" elementType="O" x2="-245330.0" y2="326750.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom5" elementType="O" x2="-166090.0" y2="-247510.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom6" elementType="P" x2="-85760.0" y2="-247510.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom7" elementType="C" x2="-245330.0" y2="81410.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom8" elementType="O" x2="-167170.0" y2="-83590.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom9" elementType="O" x2="-85760.0" y2="-327840.0" formalCharge="-1"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom10" elementType="O" x2="-327840.0" y2="-1090.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom11" elementType="C" x2="-245330.0" y2="246420.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom12" elementType="C" x2="-245330.0" y2="-1090.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom13" elementType="C" x2="-245330.0" y2="163920.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom14" elementType="C" x2="-245330.0" y2="-166090.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom15" elementType="O" x2="-85760.0" y2="-167170.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom16" elementType="O" x2="-167170.0" y2="-166090.0"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom17" elementType="O" x2="-165000.0" y2="246420.0" formalCharge="-1"/> <atom id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom18" elementType="C" x2="-245330.0" y2="-247510.0"/> </atomArray> <bondArray> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond1" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom18 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom5" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond2" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom17 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom11" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond3" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom16 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom14" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond4" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom15 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom6" order="2"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond5" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom14 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom18" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond6" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom13 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom7" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond7" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom12 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom2" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond8" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom11 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom13" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond9" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom10 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom12" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond10" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom9 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom6" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond11" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom8 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom2" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond12" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom7 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom12" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond13" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom5 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom6" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond14" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom4 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom11" order="2"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond15" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom3 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom6" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond16" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom2 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom14" order="1"/> <bond id="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-bond17" atomRefs="3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom1 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P-atom13" order="2"/> </bondArray> <formula concise="C 7 H 10 O 10 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">285.124</float> <string title="smiles">C(=O)(C(=O)CC(O)C(C(COP([O-])([O-])=O)O)O)[O-]</string> </molecule> </cml> 3-deoxy-D-arabino-heptulosonic acid 7-phosphonate 3-deoxy-D-arabino-heptulosonate-7-P 3-deoxy-arabino-heptulosonate 7-phosphate 3-deoxy-arabino-heptulosonate-7-P 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate 3-deoxy-D-arabino-hept-2-ulosonate-7-phosphate 3-deoxy-arabino-heptulonate 7-phosphate DAHP MetaCyc 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-P CAS 2627-73-8 LIGAND C04691 1 3-dehydroquinate synthase 1 1 MetaCyc 3-DEHYDROQUINATE-SYNTHASE-RXN UniProt Q9P7R0 UniProt P07639 RELATED-TO UniProt P0A4Z4 UniProt Q9JVW5 UniProt P43879 UniProt Q9PNT2 UniProt Q9CES8 UniProt P08566 RELATED-TO UniProt P07547 RELATED-TO AROBBACSU-MONOMER AroB MetaCyc AROBBACSU-MONOMER 1 REVERSIBLE 3-dehydroquinate synthase DHQ synthase dehydroquinate synthase 3-deoxy-<I>arabino</I>-heptulosonate-7-phosphate phosphate-lyase (cyclizing) MetaCyc ENZRXN-1441 Sonenshein, A.L. Hoch, J. A. Losick, R. American Society For Microbiology, Washington, DC 20005 <i>Bacillus subtilis</i> and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics 1993 58.93 Co2+ CML <cml> <molecule id="CO+2" title="Co2+" dictRef="dictCO+2"> <atomArray> <atom id="CO+2-atom1" elementType="COBALT" x2="-605.0" y2="-999.0" formalCharge="2"/> </atomArray> <bondArray> </bondArray> <formula concise="COBALT 1" formalCharge="2"/> <float title="molecularWeight" units="g/mol">58.93</float> <string title="smiles">[Co++]</string> </molecule> </cml> Co<SUP>+2</SUP> Co<SUP>++</SUP> cobalt ion MetaCyc CO+2 LIGAND C00175 CAS 7440-48-4 1 1 Dehydroquinate synthase catalyzes the cyclization of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate (DAHP) to dehydroquinate. In the course of this conversion the synthase apparently catalyzes an oxidation, a &beta;-elimination, an intramolecular aldol condensation, and a reduction |CITS:[353051],[6386050]| A common feature of the DHQ synthase activities of N. crassa and coli is a catalytic requirement for NAD+. The enzyme was shown to require catalytic amounts of NAD and Co2+. |CITS:[353051]| In the formation of DHQ, a methyl group is never formed at C-7, and the cyclization step involves an interaction between the enol formed in phosphate elimination and the carbonyl at C-2 in an aldolase-type reaction. Kinetic isotope effects were observed at C-5, supporting a mechanism involving oxidation at C-5 by NAD. The finding that all the tritium of labeled DAHP is conserved in DHQ establishes that hydride transfer involved in the subsequent reduction of C-5 uses the same hydrogen atom as was taken from DAHP. NADH is enzyme bound and reduces the keto group at C-5 with the regeneration of NAD.|CITS: [ColiSalII]| AROB-MONOMER B3389 AroB MetaCyc AROB-MONOMER UniProt P07639 RefSeq NP_417848 Pfam PF01761 IN-FAMILY Swiss-Model P07639 ModBase P07639 EcoliWiki b3389 Millar G Coggins JR PubMed 3009224 FEBS Lett 1986;200(1);11-7 The complete amino acid sequence of 3-dehydroquinate synthase of Escherichia coli K12. 1986 1 3-dehydroquinate synthase dehydroquinate synthase DHQ synthase MetaCyc 3-DEHYDROQUINATE-SYNTHASE-ENZRXN Le Marechal P Azerad R PubMed 793638 Biochimie 1976;58(9);1145-8 The shikimate pathway. IV. 3-dehydroquinate synthetase of E. coli. Substrate analogs and inhibitors. 1976 Frost JW Bender JL Kadonaga JT Knowles JR PubMed 6386050 Biochemistry 1984;23(19);4470-5 Dehydroquinate synthase from Escherichia coli: purification, cloning, and construction of overproducers of the enzyme. 1984 Rotenberg SL Sprinson DB PubMed 344312 J Biol Chem 1978;253(7);2210-5 Isotope effects in 3-dehydroquinate synthase and dehydratase. Mechanistic implications. 1978 Maitra US Sprinson DB PubMed 353051 J Biol Chem 1978;253(15);5426-30 5-Dehydro-3-deoxy-D-arabino-heptulosonic acid 7-phosphate. An intermediate in the 3-dehydroquinate synthase reaction. 1978 The aroA encoded protein is a bifunctional enzyme consisting of DAHP synthase and chorismate mutase. Both are enzymes of aromatic amino acid synthesis. There is evidence that DAHP synthase-chorismate mutase also activates another enzyme of the same pathway, shikimate kinase. |CITS: [4210506] [4211044] [6101597] [4962501] [JMB12-468] [BSUB225] [4626882]| 2.5.1.54 1 198.069 D-erythrose-4-phosphate CML <cml> <molecule id="ERYTHROSE-4P" title="D-erythrose-4-phosphate" dictRef="dictERYTHROSE-4P"> <atomArray> <atom id="ERYTHROSE-4P-atom1" elementType="C" x2="-14909.0" y2="1850.0"/> <atom id="ERYTHROSE-4P-atom2" elementType="C" x2="6525.0" y2="-2275.0"/> <atom id="ERYTHROSE-4P-atom3" elementType="C" x2="-7764.0" y2="-2275.0"/> <atom id="ERYTHROSE-4P-atom4" elementType="C" x2="-619.0" y2="1850.0"/> <atom id="ERYTHROSE-4P-atom5" elementType="P" x2="-29197.0" y2="1850.0"/> <atom id="ERYTHROSE-4P-atom6" elementType="O" x2="-33322.0" y2="-5295.0" formalCharge="-1"/> <atom id="ERYTHROSE-4P-atom7" elementType="O" x2="-36342.0" y2="5975.0" formalCharge="-1"/> <atom id="ERYTHROSE-4P-atom8" elementType="O" x2="-25072.0" y2="8994.0"/> <atom id="ERYTHROSE-4P-atom9" elementType="O" x2="-7764.0" y2="-10525.0"/> <atom id="ERYTHROSE-4P-atom10" elementType="O" x2="6525.0" y2="-10525.0"/> <atom id="ERYTHROSE-4P-atom11" elementType="O" x2="-619.0" y2="10100.0"/> <atom id="ERYTHROSE-4P-atom12" elementType="O" x2="-22052.0" y2="-2275.0"/> </atomArray> <bondArray> <bond id="ERYTHROSE-4P-bond1" atomRefs="ERYTHROSE-4P-atom5 ERYTHROSE-4P-atom8" order="2"/> <bond id="ERYTHROSE-4P-bond2" atomRefs="ERYTHROSE-4P-atom5 ERYTHROSE-4P-atom6" order="1"/> <bond id="ERYTHROSE-4P-bond3" atomRefs="ERYTHROSE-4P-atom5 ERYTHROSE-4P-atom7" order="1"/> <bond id="ERYTHROSE-4P-bond4" atomRefs="ERYTHROSE-4P-atom12 ERYTHROSE-4P-atom5" order="1"/> <bond id="ERYTHROSE-4P-bond5" atomRefs="ERYTHROSE-4P-atom11 ERYTHROSE-4P-atom4" order="1"/> <bond id="ERYTHROSE-4P-bond6" atomRefs="ERYTHROSE-4P-atom3 ERYTHROSE-4P-atom9" order="1"/> <bond id="ERYTHROSE-4P-bond7" atomRefs="ERYTHROSE-4P-atom2 ERYTHROSE-4P-atom10" order="2"/> <bond id="ERYTHROSE-4P-bond8" atomRefs="ERYTHROSE-4P-atom4 ERYTHROSE-4P-atom2" order="1"/> <bond id="ERYTHROSE-4P-bond9" atomRefs="ERYTHROSE-4P-atom3 ERYTHROSE-4P-atom4" order="1"/> <bond id="ERYTHROSE-4P-bond10" atomRefs="ERYTHROSE-4P-atom1 ERYTHROSE-4P-atom3" order="1"/> <bond id="ERYTHROSE-4P-bond11" atomRefs="ERYTHROSE-4P-atom12 ERYTHROSE-4P-atom1" order="1"/> </bondArray> <formula concise="C 4 H 7 O 7 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">198.069</float> <string title="smiles">C(OP([O-])([O-])=O)C(C(C=O)O)O</string> </molecule> </cml> erythrose-4P threose 4-phosphate erythrose-4-phosphate erythrose-4-P D-erythrose-4-P MetaCyc ERYTHROSE-4P CAS 585-18-2 LIGAND C00279 PubChem 122357 1 1 2-dehydro-3-deoxyphosphoheptonate aldolase 1 1 KDPH synthase DHAP synthase Phospho-2-keto-3-deoxyheptonate aldolase Phospho-2-dehydro-3-deoxyheptonate aldolase MetaCyc DAHPSYN-RXN UniProt O52798 UniProt O22407 UniProt Q42921 UniProt P29976 UniProt Q00218 UniProt Q09755 UniProt P37216 UniProt P37215 UniProt P32449 UniProt Q02285 UniProt P14843 UniProt P39912 UniProt P34725 UniProt P44303 UniProt P35170 UniProt P46245 UniProt Q9PPJ1 UniProt P00888 RELATED-TO UniProt P0AB91 RELATED-TO UniProt P00887 RELATED-TO UniProt Q9JSQ8 UniProt P0A1B5 AroA AroA MetaCyc AROABACSU-MONOMER 4 CPLX-1101 MetaCyc CPLX-1101 1 REVERSIBLE DAHP synthase 3-deoxy-D-<I>arabino</I>-heptulosonate 7-phosphate synthase 2-dehydro-3-deoxy-D-<I>arabino</I>-heptonate-7-phosphate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating) MetaCyc ENZRXN-1401 55.847 Fe2+ CML <cml> <molecule id="FE+2" title="Fe2+" dictRef="dictFE+2"> <atomArray> <atom id="FE+2-atom1" elementType="FE" x2="-962.0" y2="-999.0" formalCharge="2"/> </atomArray> <bondArray> </bondArray> <formula concise="FE 1" formalCharge="2"/> <float title="molecularWeight" units="g/mol">55.847</float> <string title="smiles">[Fe++]</string> </molecule> </cml> Fe<SUP>+2</SUP> Fe<SUP>++</SUP> ferrous iron Fe+2 Fe2+ Fe(II) MetaCyc FE+2 LIGAND C00023 1 Control of aromatic amino acid biosynthesis is exerted on the first and fifth steps of the shared or common pathway as well as all the enzymes of the terminal pathways. The common aromatic biosynthetic pathway consists of seven steps of which the first one, DAHP synthase, represents the major control point for carbon flow through this pathway. |CITS:[6146618]| There are 3 DAHP synthases. The aroF isozyme is feedback inhibited by tyrosine. The other two are phe and trp sensitive. The three isozymes provide the cell with the ability to modulate the overall rate of synthesis in response to change in the availability of particular amino acids. In addition to feedback inhibition, the synthesis of DAHP (tyr) is repressed by high levels of phenylalanine. Product inhibition studies reveal that P-enolpyruvate is the first substrate to bind the enzyme, and that inorganic phosphate is the first product to dissociate from the E-P-Q complex. All three DAHP synthases have been shown to contain 1 mol of iron per mol of native enzyme and DAHP synthase (tyr) contains a short amino acid sequence which is highly homologous with a putative iron-binding sequence in hemerythrin, the oxygen carrying molecule in the sea worm Phascolopsis gouldii. When coli grows in minimal medium, DAHP synthase(phe) comprises about 80% or more of total DAHP synthase actvity; however, under conditions in which the aromatic amino acids limit growth, as in minimal medium supplemented with all amino acids except phenylalanine, tyrosine and tryptophan, derepression of DAHP synthase (tyr)makes it the major enzyme. A similar situation occurs when cells are starved for iron. DAHP synthase (phe) is also the major isoenzyme present when S. typhimurium is grown in minimal medium, although there is one report of high levels of DAHP synthase (tyr) under these conditions. In both organisms, DAHP synthase(trp) normally accounts for a very small proportion of DAHP synthase activity.|CITS:[ColiSalII]| aroF and tyrA encoding the bifunctional chorismate mutase prephenate dehydrogenase form the tyrosine operon. The tyrosine operon is repressed by tyrosine and phenylalanine. This repression is mediated by the tyrR gene product postulated to bind at a regulatory region preceding the aroF coding sequence. AroF B2601 AroF MetaCyc AROF-MONOMER UniProt P00888 RefSeq NP_417092 Pfam PF00793 IN-FAMILY Swiss-Model P00888 ModBase P00888 EcoliWiki b2601 Ray JM Yanofsky C Bauerle R PubMed 2903857 J Bacteriol 1988;170(12);5500-6 Mutational analysis of the catalytic and feedback sites of the tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase of Escherichia coli. 1988 2 AROF-CPLX MetaCyc AROF-CPLX 1 REVERSIBLE 2-dehydro-3-deoxyphosphoheptonate aldolase Phospho-2-keto-3-deoxyheptonate aldolase DHAP synthase DHAPS KDPH synthetase tyrosine sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (tyr) MetaCyc DAHPSYNTYR-ENZRXN Shultz J Hermodson MA Garner CC Herrmann KM PubMed 6146618 J Biol Chem 1984;259(15);9655-61 The nucleotide sequence of the aroF gene of Escherichia coli and the amino acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. 1984 Schoner R Herrmann KM PubMed 9387 J Biol Chem 1976;251(18);5440-7 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli. 1976 Herrmann KM Shultz J Hermodson MA PubMed 6104668 J Biol Chem 1980;255(15);7079-81 Sequence homology between the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli and hemerythrin from Sipunculida. 1980 The presence of three isozymes provides coli with the capability for tight, multivalent regulation of the first step toward aromatic amino acid biosynthesis, while allowing sufficient residual enzyme activity in the presence of excess aromatic amino acids to provide for the synthesis of the other aromatic compounds. The aroH DAHP synthase contributes only about 1% of the total activity. |CITS: [6396419]| Although catalyzing the same reaction, each isozyme is feedback-regulated by a different aromatic amino acid. The three genes are widely separated on the coli chromosome. |CITS:[2903857]| The aroH gene has two promoters. One is regulated by the trp repressor and is favored by growth on minimal media. The other promoter is activated under conditions of growth in rich medium by an unknown mechanism. The presence of a second promoter that is active during growth in the presence of high levels of aromatic amino acid could allow aroH to escape from repression and ensure a low level of metabolic flux through the shikimate pathway for the biosynthesis of aromatic vitamins not present in the growth medium. Of the three isozymes, DAHP synthase (Trp) is only moderately feedback-inhibited and will function despite high levels of intracellular tryptophan |CITS:[1677907]|. In wild-type cells grown in minimal medium, the aroG isozyme makes up about 80% of the total DAHPS activity, the aroF isozyme makes up 20%, and the aroH isozyme makes up about 1%. AroH B1704 AroH MetaCyc AROH-MONOMER UniProt P00887 RefSeq NP_416219 Pfam PF00793 IN-FAMILY Swiss-Model P00887 ModBase P00887 EcoliWiki b1704 2 AROH-CPLX MetaCyc AROH-CPLX 1 REVERSIBLE 2-dehydro-3-deoxyphosphoheptonate aldolase phospho-2-keto-3-deoxyheptonate aldolase DHAP synthase DHAPS KDPH synthetase tryptophan sensitive 3-deoxy-D arabino-heptulosonate 7-phosphate synthase 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (trp) MetaCyc DAHPSYNTRP-ENZRXN Zurawski G Gunsalus RP Brown KD Yanofsky C PubMed 6167722 J Mol Biol 1981;145(1);47-73 Structure and regulation of aroH, the structural gene for the tryptophan-repressible 3-deoxy-D-arabino-heptulosonic acid-7-phosphate synthetase of Escherichia coli. 1981 Camakaris J Pittard J PubMed 4939760 J Bacteriol 1971;107(2);406-14 Repression of 3-deoxy-D-arabinoheptulosonic acid-7-phosphate synthetase (trp) and enzymes of the tryptophan pathway in Escherichia coli K-12. 1971 Camakaris J Pittard J PubMed 4218228 J Bacteriol 1974;120(2);590-7 Purification and properties of 3-deoxy-D-arabionheptulosonic acid-7-phosphate synthetase (trp) from Escherichia coli. 1974 Hudson GS Rellos P Davidson BE PubMed 1677907 Gene 1991;102(1);87-91 Two promoters control the aroH gene of Escherichia coli. 1991 Akowski JP Bauerle R PubMed 9398312 Biochemistry 1997;36(50);15817-22 Steady-state kinetics and inhibitor binding of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tryptophan sensitive) from Escherichia coli. 1997 1 The presence of three isoenzymes provides coli with the capability for tight, multivalent regulation of the first step towards aromatic biosynthesis, while allowing sufficient residual enzyme activity in the presence of excess aromatic amino acids to provide for the synthesis of the other aromatic compounds.|CITS:[6396419]| Although catalyzing the same reaction, each isoenzyme is feedback regulated by a different aromatic amino acid.|CITS: [2903857]| Isozymes provides the cell with the ability to modulate the overall rate of synthesis in response to changes in the availability of particular amino acids. In addition to feedback inhibition, the synthesis of DAHP(phe) is repressed by phenylalanine and tryptophan. When coli grows in minimal medium, DAHP synthase (Phe) comprises about 80% or more of total DAHP synthase activity; however, under conditions in which the aromatic amino acids limit growth, as in minmal medium supplemented with all amino acids except phenylalanine, tyrosine, and tryptophan, derepression of DAHP synthase (tyr) makes it the major enzyme. A similar situation occurs when cells are starved for iron. DAHP synthase (trp) normally accounts for a very small proportion of DAHP activity. In vivo studies with mutant strains containing single isoenzymes have shown that, in the presence of all three aromatic amino acids, the cell retains enough residual activity of both DAHP synthase (phe) and DAHP synthase (trp) to allow for continued synthesis of the aromatic vitamins. Transcription of the isozymes is regulated by repression, with the end products of the pathway acting as co-repressors |CITS:[6125934]|The binding of phosphoenolpyruvate (PEP) to the enzyme requires a phosphoryl group on the C-2 position of the substrate and one free hydrogen atom at the C-3 position. The mechanism is ordered and sequential. PEP is the first substrate to bind. Each isozyme contains 1 mol of iron per mol of native enzyme. The pattern obtained (competitive inhibition when PEP was the variable substrate and non-competitive inhibition when erythrose-4-phosphate was the varible substrate) indicates that the reaction mechanism cannot be ping pong. This pattern is consistent with an ordered sequential mechanism for ths enzyme, but does not in itself exclude the other ordered mechanisms.|CITS: [12952]| Expression of aroF and aroG is repressed by the tyrR protein with tyrosine or phenylalanine plus tryptophan, respectively as corepressors The three genes (aroF, aroG and aroH) are widely separated on the coli chromosome. In wild-type cells grown in minimal mediuim, the AroG enzyme makes up about 80% of the total DAHPS activity, the AroF isoenzyme makes up 20%, and the AroH isoenzyme makes up about 1% |CITS:[2903857]|. AroG B0754 AroG MetaCyc AROG-MONOMER PDB 1GG1 PDB 1KFL RefSeq NP_415275 UniProt P0AB91 PDB 1QR7 Pfam PF00793 IN-FAMILY ModBase P0AB91 EcoliWiki b0754 McCandliss RJ Poling MD Herrmann KM PubMed 26682 J Biol Chem 1978;253(12);4259-65 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli. 1978 4 AROG-CPLX MetaCyc AROG-CPLX 1 REVERSIBLE 2-dehydro-3-deoxyphosphoheptonate aldolase Phospho-2-keto-3-deoxyheptonate aldolase DHAP synthase DHAPS KDPH synthetase phenylalanine sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase(pyruvate phosphorylating) 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) MetaCyc DAHPSYNPHE-ENZRXN Davies WD Davidson BE PubMed 6125934 Nucleic Acids Res 1982;10(13);4045-8 The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12. 1982 Simpson RJ Davidson BE PubMed 12952 Eur J Biochem 1976;70(2);501-7 Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe)from Escherichia coli K12. 2. Kinetic properties. 1976 Kinetic parameters have been measured by different authors. The K_m for NAD is 87 &micro;M, and the K_m for NADP is 100 &micro;M. The enzyme has a lower K_m for shikimate in the presence of NAD |CITS: [12637497]|. The K_m for NAD was also reported to be 12.2 &micro;M |CITS: [15596430]|. The K_cat of YdiB is reported to be about 4000-fold lower |CITS: [12637497]| or only 7-fold lower |CITS: [12624088]| than that of AroE. The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term '5-dehydroquinate' for this compound is based on an earlier system of numbering. 1.1.1.282 1 NAD(P)⁺ is a class of compounds including the instances NAD⁺ and NADP⁺. 0.0 NAD(P)+ NAD(P) NAD(P)+ MetaCyc NAD-P-OR-NOP 1 quinate/shikimate dehydrogenase 1 NAD(P)H is a class of compounds including the instances NADH and NADPH. 2.016 NAD(P)H MetaCyc NADH-P-OR-NOP 1 1 MetaCyc RXN-7968 The <i>ydiB</i> gene encodes a quinate/shikimate dehydrogenase |CITS: [12637497]|. NAD copurifies with YdiB |CITS: [12624088]|. The enzyme can use both NAD or NADP for catalysis, but has higher catalytic efficiency with NAD |CITS: [12637497]|. Because the intracellular concentration of NAD is reported to be 40-fold higher than that of NADH, it is suggested that the dehydrogenase direction is favored by YdiB <i>in vivo</i> |CITS: [16828913]|. Crystal structures of the enzyme are presented at 2.3 &Aring; resolution |CITS: [12624088]| and 2.5 &Aring; resolution |CITS: [12637497]|. The structure is discussed with respect to the enzyme catalytic mechanism |CITS: [12624088][12637497]|. However, site-directed mutagenesis of predicted active-site residues suggested that catalysis does not involve a general acid-base mechanism |CITS: [15596430]|. EG11234-MONOMER B1692 YdiB MetaCyc EG11234-MONOMER PDB 1NPD RefSeq NP_416207 PDB 1VI2 Structure Pfam PF01488 IN-FAMILY UniProt P0A6D5 ModBase P0A6D5 PDB 1O9B EcoliWiki b1692 2 CPLX0-7462 MetaCyc CPLX0-7462 1 REVERSIBLE shikimate dehydrogenase MetaCyc ENZRXN0-3081 Indole-3-glycerol phosphate synthase catalyzes the fourth reaction in the tryptophan biosynthetic pathway. |CITS: [10329177] [7556082]| 4.1.1.48 1 346.21 1-(o-carboxyphenylamino)-1'-deoxyribulose-5'-phosphate CML <cml> <molecule id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P" title="1-(o-carboxyphenylamino)-1'-deoxyribulose-5'-phosphate" dictRef="dictCARBOXYPHENYLAMINO-DEOXYRIBULOSE-P"> <atomArray> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom1" elementType="C" x2="-31179.0" y2="17894.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom2" elementType="C" x2="-24108.0" y2="-15106.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom3" elementType="O" x2="-15000.0" y2="-23035.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom4" elementType="C" x2="-23787.0" y2="31073.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom5" elementType="O" x2="-1394.0" y2="23571.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom6" elementType="P" x2="-6856.0" y2="-23035.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom7" elementType="N" x2="-23677.0" y2="9107.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom8" elementType="C" x2="-24108.0" y2="2787.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom9" elementType="C" x2="-16285.0" y2="18751.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom10" elementType="C" x2="-24108.0" y2="-23035.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom11" elementType="O" x2="-15964.0" y2="2787.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom12" elementType="O" x2="-3966.0" y2="11680.0" formalCharge="-1"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom13" elementType="C" x2="-23677.0" y2="14464.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom14" elementType="C" x2="-31179.0" y2="26465.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom15" elementType="O" x2="-16179.0" y2="-15106.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom16" elementType="C" x2="-8035.0" y2="18751.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom17" elementType="C" x2="-27859.0" y2="6108.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom18" elementType="O" x2="-6856.0" y2="-14894.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom19" elementType="C" x2="-24108.0" y2="-6535.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom20" elementType="O" x2="-6856.0" y2="-31179.0" formalCharge="-1"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom21" elementType="O" x2="-16179.0" y2="-6535.0"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom22" elementType="O" x2="1285.0" y2="-23035.0" formalCharge="-1"/> <atom id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom23" elementType="C" x2="-16285.0" y2="26465.0"/> </atomArray> <bondArray> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond1" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom4 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom23" order="2"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond2" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom23 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom9" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond3" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom22 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom6" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond4" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom21 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom19" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond5" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom20 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom6" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond6" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom19 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom2" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond7" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom18 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom6" order="2"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond8" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom17 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom8" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond9" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom16 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom9" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond10" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom15 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom2" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond11" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom1 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom14" order="2"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond12" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom13 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom7" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond13" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom12 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom16" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond14" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom11 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom8" order="2"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond15" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom10 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom3" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond16" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom9 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom13" order="2"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond17" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom8 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom19" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond18" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom7 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom17" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond19" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom5 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom16" order="2"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond20" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom14 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom4" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond21" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom3 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom6" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond22" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom2 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom10" order="1"/> <bond id="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-bond23" atomRefs="CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom13 CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P-atom1" order="1"/> </bondArray> <formula concise="C 12 H 13 N 1 O 9 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">346.21</float> <string title="smiles">C(C(O)C(C(=O)CNC1(C=CC=CC=1C(=O)[O-]))O)OP(=O)([O-])[O-]</string> </molecule> </cml> 1-(o-carboxyphenylamino)-1'-deoxyribulose-5'-P 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-P MetaCyc CARBOXYPHENYLAMINO-DEOXYRIBULOSE-P LIGAND C01302 1 indole-3-glycerol-phosphate synthase 285.193 indole-3-glycerol-phosphate CML <cml> <molecule id="INDOLE-3-GLYCEROL-P" title="indole-3-glycerol-phosphate" dictRef="dictINDOLE-3-GLYCEROL-P"> <atomArray> <atom id="INDOLE-3-GLYCEROL-P-atom1" elementType="C" x2="-10214.0" y2="15509.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom2" elementType="C" x2="-18063.0" y2="4823.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom3" elementType="P" x2="2175.0" y2="-17589.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom4" elementType="C" x2="-10214.0" y2="8985.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom5" elementType="O" x2="17212.0" y2="-4539.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom6" elementType="C" x2="2175.0" y2="-4823.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom7" elementType="O" x2="17022.0" y2="8795.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom8" elementType="O" x2="9837.0" y2="-17589.0" formalCharge="-1"/> <atom id="INDOLE-3-GLYCEROL-P-atom9" elementType="O" x2="2175.0" y2="-12105.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom10" elementType="O" x2="-5579.0" y2="-17589.0" formalCharge="-1"/> <atom id="INDOLE-3-GLYCEROL-P-atom11" elementType="C" x2="2365.0" y2="15509.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom12" elementType="C" x2="-18063.0" y2="19766.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom13" elementType="C" x2="9930.0" y2="5675.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom14" elementType="C" x2="-25345.0" y2="15793.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom15" elementType="C" x2="9930.0" y2="-1703.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom16" elementType="C" x2="-25345.0" y2="8701.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom17" elementType="N" x2="-3878.0" y2="19102.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom18" elementType="C" x2="2365.0" y2="8985.0"/> <atom id="INDOLE-3-GLYCEROL-P-atom19" elementType="O" x2="2175.0" y2="-25345.0"/> </atomArray> <bondArray> <bond id="INDOLE-3-GLYCEROL-P-bond1" atomRefs="INDOLE-3-GLYCEROL-P-atom18 INDOLE-3-GLYCEROL-P-atom4" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond2" atomRefs="INDOLE-3-GLYCEROL-P-atom17 INDOLE-3-GLYCEROL-P-atom11" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond3" atomRefs="INDOLE-3-GLYCEROL-P-atom16 INDOLE-3-GLYCEROL-P-atom14" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond4" atomRefs="INDOLE-3-GLYCEROL-P-atom15 INDOLE-3-GLYCEROL-P-atom13" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond5" atomRefs="INDOLE-3-GLYCEROL-P-atom14 INDOLE-3-GLYCEROL-P-atom12" order="2"/> <bond id="INDOLE-3-GLYCEROL-P-bond6" atomRefs="INDOLE-3-GLYCEROL-P-atom13 INDOLE-3-GLYCEROL-P-atom7" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond7" atomRefs="INDOLE-3-GLYCEROL-P-atom13 INDOLE-3-GLYCEROL-P-atom18" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond8" atomRefs="INDOLE-3-GLYCEROL-P-atom12 INDOLE-3-GLYCEROL-P-atom1" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond9" atomRefs="INDOLE-3-GLYCEROL-P-atom11 INDOLE-3-GLYCEROL-P-atom18" order="2"/> <bond id="INDOLE-3-GLYCEROL-P-bond10" atomRefs="INDOLE-3-GLYCEROL-P-atom10 INDOLE-3-GLYCEROL-P-atom3" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond11" atomRefs="INDOLE-3-GLYCEROL-P-atom9 INDOLE-3-GLYCEROL-P-atom6" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond12" atomRefs="INDOLE-3-GLYCEROL-P-atom6 INDOLE-3-GLYCEROL-P-atom15" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond13" atomRefs="INDOLE-3-GLYCEROL-P-atom5 INDOLE-3-GLYCEROL-P-atom15" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond14" atomRefs="INDOLE-3-GLYCEROL-P-atom4 INDOLE-3-GLYCEROL-P-atom2" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond15" atomRefs="INDOLE-3-GLYCEROL-P-atom3 INDOLE-3-GLYCEROL-P-atom19" order="2"/> <bond id="INDOLE-3-GLYCEROL-P-bond16" atomRefs="INDOLE-3-GLYCEROL-P-atom3 INDOLE-3-GLYCEROL-P-atom8" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond17" atomRefs="INDOLE-3-GLYCEROL-P-atom3 INDOLE-3-GLYCEROL-P-atom9" order="1"/> <bond id="INDOLE-3-GLYCEROL-P-bond18" atomRefs="INDOLE-3-GLYCEROL-P-atom2 INDOLE-3-GLYCEROL-P-atom16" order="2"/> <bond id="INDOLE-3-GLYCEROL-P-bond19" atomRefs="INDOLE-3-GLYCEROL-P-atom1 INDOLE-3-GLYCEROL-P-atom4" order="2"/> <bond id="INDOLE-3-GLYCEROL-P-bond20" atomRefs="INDOLE-3-GLYCEROL-P-atom1 INDOLE-3-GLYCEROL-P-atom17" order="1"/> </bondArray> <formula concise="C 11 H 12 N 1 O 6 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">285.193</float> <string title="smiles">C(C(O)C(C2(=CNC1(=C(C=CC=C1)2)))O)OP([O-])(=O)[O-]</string> </molecule> </cml> C¹-(3-Indolyl)-glycerol 3-phosphate indole-3-glycerol-P 1-(indol-3-yl)glycerol-3-P 1-(indol-3-yl)glycerol-3-phosphate indoleglycerol phosphate MetaCyc INDOLE-3-GLYCEROL-P LIGAND C03506 1 44.01 CO2 CML <cml> <molecule id="CARBON-DIOXIDE" title="CO2" dictRef="dictCARBON-DIOXIDE"> <atomArray> <atom id="CARBON-DIOXIDE-atom1" elementType="C" x2="-1100.0" y2="-826100.0"/> <atom id="CARBON-DIOXIDE-atom2" elementType="O" x2="-826100.0" y2="-826100.0"/> <atom id="CARBON-DIOXIDE-atom3" elementType="O" x2="823900.0" y2="-823900.0"/> </atomArray> <bondArray> <bond id="CARBON-DIOXIDE-bond1" atomRefs="CARBON-DIOXIDE-atom3 CARBON-DIOXIDE-atom1" order="2"/> <bond id="CARBON-DIOXIDE-bond2" atomRefs="CARBON-DIOXIDE-atom2 CARBON-DIOXIDE-atom1" order="2"/> </bondArray> <formula concise="C 1 O 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">44.01</float> <string title="smiles">C(=O)=O</string> </molecule> </cml> carbonic anhydride carbonic acid gas carbon dioxide MetaCyc CARBON-DIOXIDE CAS 124-38-9 LIGAND C00011 ChEBI 16526 LIGAND C00011 PubChem 280 1 1 Indoleglycerol phosphate synthase indole-3-glycerol phosphate synthesis MetaCyc IGPSYN-RXN UniProt P94327 UniProt Q9ZFA7 UniProt Q92370 RELATED-TO UniProt Q9X7C7 UniProt Q9S591 UniProt Q9YGB5 RELATED-TO UniProt Q01999 UniProt P24773 RELATED-TO UniProt P26938 UniProt P25170 RELATED-TO UniProt P18483 RELATED-TO UniProt P06531 RELATED-TO UniProt P05328 RELATED-TO UniProt P00908 RELATED-TO UniProt P00937 RELATED-TO UniProt P20409 RELATED-TO UniProt P17217 UniProt P00911 UniProt P00909 RELATED-TO UniProt P00910 RELATED-TO UniProt P03964 UniProt Q9JSN4 UniProt Q58328 UniProt Q9PI11 UniProt P20578 UniProt Q9V1G3 UniProt Q06121 RELATED-TO UniProt P18304 UniProt P20577 UniProt P42393 RELATED-TO MONOMER-343 Thermotoga maritima NCBI Taxonomy 2336 TrpC Indoglycerol phosphate synthase tIGPS MetaCyc MONOMER-343 UniProt Q56319 Swiss-Model Q56319 ModBase Q56319 PDB 1J5T PDB 1I4N Merz A Knochel T Jansonius JN Kirschner K PubMed 10329177 J Mol Biol 1999;288(4);753-63 The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges. 1999 1 IRREVERSIBLE-LEFT-TO-RIGHT indole-3-glycerol phosphate synthase 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase (cyclizing) MetaCyc ENZRXN-2663 indole-3-glycerol phosphate synthase Thermococcus kodakarensis NCBI Taxonomy 311400 TrpC InGPS MetaCyc MONOMER-3581 UniProt Q9YGB5 Swiss-Model Q9YGB5 ModBase Q9YGB5 Tang X Ezaki S Fujiwara S Takagi M Atomi H Imanaka T PubMed 10628865 Mol Gen Genet 262(4-5);815-21 The tryptophan biosynthesis gene cluster trpCDEGFBA from Pyrococcus kodakaraensis KOD1 is regulated at the transcriptional level and expressed as a single mRNA. 1999 1 indole-3-glycerol phosphate synthase MetaCyc ENZRXN-3684 indole-3-glycerol phosphate synthase Sulfolobus solfataricus NCBI Taxonomy 2287 TrpC IndGroP synthase MetaCyc MONOMER-3602 UniProt Q06121 Swiss-Model Q06121 ModBase Q06121 PDB 1LBL PDB 1LBF PDB 1JUL PDB 1JUK PDB 1IGS PDB 1A53 1 indole-3-glycerol phosphate synthase MetaCyc ENZRXN-3701 No cofactors or metal ions have been identified as essential for catalysis |CITS: [2494074]|. Bifunctional phosphoribosylanthranilate isomerase / indole-3-glycerol phosphate synthase (TrpC) carries out the third and fourth steps in the tryptophan biosynthesis pathway. The phosphoribosylanthranilate isomerase activity of TrpC catalyzes the Amadori rearrangement of its substrate into carboxyphenylaminodeoxyribulose phosphate |CITS: [Febslett14887-90][4865047]|. The indole-glycerol phosphate synthase activity of TrpC catalyzes the ring closure of this product to yield indole-3-glycerol phosphate |CITS: [Febslett14887-90][4865047][5332729]|. A number of structural studies show that TrpC has two individual domains, each catalyzing one of its two activities. Crystal structures to 2, 2.8, and 4 &Aring; resolution, as well as protease studies, show that the two TrpC domains are distinct, each with a folding pattern of an 8-fold parallel &beta;-&alpha; barrel |CITS: [7014916][3303031][2494074][2184433][1738159]|. The amino-terminal domain carries out the synthase activity and the carboxy-terminal domain carries out the isomerase activity |CITS: [2494074]|. The two active sites face away from each other, presumably precluding direct transfer of carboxyphenylaminodeoxyribulose phosphate from the isomerase site to the synthase site |CITS: [3303031]|. The isolated synthase domain is unstable, suggesting that the combined domains may mutually stabilize each other |CITS: [7014916][3303031]|. TrpC is unique among the five enzymes in the tryptophan biosynthesis pathway in that it is not part of a multisubunit enzyme complex |CITS: [7007653]|. PRAI-IGPS B1262 TrpC TrpF MetaCyc PRAI-IGPS UniProt P00909 RefSeq NP_415778 PDB 1PII Pfam PF00218 IN-FAMILY ModBase P00909 EcoliWiki b1262 1 indole-3-glycerol phosphate synthase IGP synthase MetaCyc IGPSYN-ENZRXN Phosphoribosyl anthranilate isomerase (tPRAI) catalyzes the third reaction in the tryptophan biosynthetic pathway. Unlike most of the tPRAIs from mesophilic organisms, the Termotoga maritima enzyme is a homodimer. 5.3.1.24 346.21 N-(5'-phosphoribosyl)-anthranilate CML <cml> <molecule id="N-5-PHOSPHORIBOSYL-ANTHRANILATE" title="N-(5'-phosphoribosyl)-anthranilate" dictRef="dictN-5-PHOSPHORIBOSYL-ANTHRANILATE"> <atomArray> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom1" elementType="C" x2="69920.0" y2="18610.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom2" elementType="N" x2="193670.0" y2="-43760.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom3" elementType="C" x2="141350.0" y2="58850.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom4" elementType="C" x2="1510.0" y2="141350.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom5" elementType="O" x2="-223850.0" y2="-36720.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom6" elementType="C" x2="193670.0" y2="-174560.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom7" elementType="P" x2="-223850.0" y2="-122240.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom8" elementType="C" x2="-23640.0" y2="-174560.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom9" elementType="C" x2="151420.0" y2="-258060.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom10" elementType="C" x2="222850.0" y2="184620.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom11" elementType="O" x2="222850.0" y2="270130.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom12" elementType="O" x2="-309370.0" y2="-122240.0" formalCharge="-1"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom13" elementType="C" x2="141350.0" y2="141350.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom14" elementType="C" x2="1510.0" y2="58850.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom15" elementType="O" x2="308370.0" y2="184620.0" formalCharge="-1"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom16" elementType="O" x2="86020.0" y2="-114190.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom17" elementType="O" x2="-143370.0" y2="-122240.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom18" elementType="C" x2="-23640.0" y2="-122240.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom19" elementType="C" x2="17610.0" y2="-258060.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom20" elementType="O" x2="-223850.0" y2="-207760.0" formalCharge="-1"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom21" elementType="O" x2="17610.0" y2="-309370.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom22" elementType="O" x2="151420.0" y2="-309370.0"/> <atom id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom23" elementType="C" x2="69920.0" y2="181600.0"/> </atomArray> <bondArray> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond1" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom23 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom13" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond2" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom22 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom9" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond3" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom21 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom19" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond4" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom20 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom7" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond5" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom19 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom9" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond6" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom18 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom8" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond7" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom17 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom18" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond8" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom16 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom6" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond9" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom15 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom10" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond10" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom1 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom14" order="2"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond11" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom13 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom3" order="2"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond12" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom12 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom7" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond13" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom11 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom10" order="2"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond14" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom10 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom13" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond15" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom8 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom19" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond16" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom8 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom16" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond17" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom7 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom17" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond18" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom6 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom9" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond19" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom5 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom7" order="2"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond20" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom4 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom23" order="2"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond21" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom14 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom4" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond22" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom3 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom2" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond23" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom2 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom6" order="1"/> <bond id="N-5-PHOSPHORIBOSYL-ANTHRANILATE-bond24" atomRefs="N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom3 N-5-PHOSPHORIBOSYL-ANTHRANILATE-atom1" order="1"/> </bondArray> <formula concise="C 12 H 13 N 1 O 9 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">346.21</float> <string title="smiles">C2(NC1(C=CC=CC(C(=O)[O-])=1))(C(C(C(O2)COP(=O)([O-])[O-])O)O)</string> </molecule> </cml> <i>N</i>-(5-phospho-D-ribosyl)-anthranilate <i>N</i>-(5-phospho-&beta;-D-ribosyl)-anthranilate 5-phosphoribosyl-anthranilate 5-P-ribosyl-anthranilate 5'-phosphoribosyl-anthranilate 5'-P-ribosyl-anthranilate <i>N</i>-(5-phosphoribosyl)-anthranilate MetaCyc N-5-PHOSPHORIBOSYL-ANTHRANILATE LIGAND C04302 1 Phosphoribosylanthranilate isomerase 1 PRAI N-(5'-phosphoribosyl)anthranilate isomerase phosphoribosylanthranilate isomerization MetaCyc PRAISOM-RXN UniProt Q9YGB1 UniProt P74435 UniProt Q01128 UniProt Q56320 RELATED-TO UniProt Q02002 UniProt P18483 RELATED-TO UniProt P00908 RELATED-TO UniProt P17218 UniProt P27710 UniProt P50857 UniProt P13997 UniProt P00912 UniProt P00909 RELATED-TO UniProt P00910 RELATED-TO UniProt Q9JVD1 UniProt P20167 UniProt Q57893 UniProt Q9PIF3 UniProt P42393 RELATED-TO UniProt P12289 UniProt O67853 UniProt P16923 phosphoribosylanthranilate isomerase subunit TrpF MetaCyc MONOMER-301 UniProt Q56320 Swiss-Model Q56320 ModBase Q56320 PDB 1NSJ PDB 1LBM Bairoch A Boeckman B Nucleic Acids Res. 21:3093-3096 The SWISS-PROT protein sequence data bank, recent developments 2 CPLX-1801 tPRAI phophoribosyl anthranilate isomerase MetaCyc CPLX-1801 Sterner R Kleemann GR Szadkowski H Lustig A Hennig M Kirschner K PubMed 8897600 Protein Sci 1996;5(10);2000-8 Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer. 1996 1 IRREVERSIBLE-LEFT-TO-RIGHT phosphoribosylanthranilate isomerase <I>N</I>-(5'-phosphoribosyl)anthranilate isomerase <I>N</I>-(5-phospho-&beta;-D-ribosyl)anthranilate ketol-isomerase MetaCyc ENZRXN-2621 Sterner R Dahm A Darimont B Ivens A Liebl W Kirschner K PubMed 7556082 EMBO J 1995;14(18);4395-402 (Beta alpha)8-barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima. 1995 1 phosphoribosylanthranilate isomerase PRA isomerase PRAI N-(5'-phosphoribosyl) anthranilate isomerase MetaCyc PRAISOM-ENZRXN The gene trpDG encodes a protein with two enzymatic activities. On its own it catalyzes the anthranilate phosphoribosyltransferase reaction, the second reaction in the tryptophan biosynthetic pathway. As anthranilate synthase component II it provides the amidotransferase activity in the anthranilate synthase reaction in conjunction with component I. 2.4.2.18 1 174.951 diphosphate CML <cml> <molecule id="PPI" title="diphosphate" dictRef="dictPPI"> <atomArray> <atom id="PPI-atom1" elementType="O" x2="-1140.0" y2="-87050.0"/> <atom id="PPI-atom2" elementType="O" x2="86480.0" y2="-4550.0"/> <atom id="PPI-atom3" elementType="O" x2="86480.0" y2="-169550.0"/> <atom id="PPI-atom4" elementType="P" x2="86480.0" y2="-87050.0"/> <atom id="PPI-atom5" elementType="O" x2="-169550.0" y2="-87050.0" formalCharge="-1"/> <atom id="PPI-atom6" elementType="O" x2="-87050.0" y2="-169550.0" formalCharge="-1"/> <atom id="PPI-atom7" elementType="O" x2="168980.0" y2="-87050.0" formalCharge="-1"/> <atom id="PPI-atom8" elementType="P" x2="-87050.0" y2="-87050.0"/> <atom id="PPI-atom9" elementType="O" x2="-87050.0" y2="-4550.0"/> </atomArray> <bondArray> <bond id="PPI-bond1" atomRefs="PPI-atom9 PPI-atom8" order="2"/> <bond id="PPI-bond2" atomRefs="PPI-atom7 PPI-atom4" order="1"/> <bond id="PPI-bond3" atomRefs="PPI-atom6 PPI-atom8" order="1"/> <bond id="PPI-bond4" atomRefs="PPI-atom5 PPI-atom8" order="1"/> <bond id="PPI-bond5" atomRefs="PPI-atom4 PPI-atom1" order="1"/> <bond id="PPI-bond6" atomRefs="PPI-atom3 PPI-atom4" order="1"/> <bond id="PPI-bond7" atomRefs="PPI-atom2 PPI-atom4" order="2"/> <bond id="PPI-bond8" atomRefs="PPI-atom1 PPI-atom8" order="1"/> </bondArray> <formula concise="H 1 O 7 P 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">174.951</float> <string title="smiles">O(P([O-])([O-])=O)P(=O)(O)[O-]</string> </molecule> </cml> diphosphate PPi PP pyrophosphate MetaCyc PPI CAS 2466-09-3 LIGAND C00013 CAS 09/03/2466 1 Anthranilate phosphoribosyltransferase 136.13 anthranilate CML <cml> <molecule id="ANTHRANILATE" title="anthranilate" dictRef="dictANTHRANILATE"> <atomArray> <atom id="ANTHRANILATE-atom1" elementType="C" x2="-12227.0" y2="-4837.0"/> <atom id="ANTHRANILATE-atom2" elementType="C" x2="-5083.0" y2="-711.0"/> <atom id="ANTHRANILATE-atom3" elementType="C" x2="2062.0" y2="-4837.0"/> <atom id="ANTHRANILATE-atom4" elementType="C" x2="2062.0" y2="-13087.0"/> <atom id="ANTHRANILATE-atom5" elementType="C" x2="-12227.0" y2="-13087.0"/> <atom id="ANTHRANILATE-atom6" elementType="C" x2="-19372.0" y2="-17212.0"/> <atom id="ANTHRANILATE-atom7" elementType="C" x2="-5083.0" y2="-17212.0"/> <atom id="ANTHRANILATE-atom8" elementType="N" x2="-5083.0" y2="-25462.0"/> <atom id="ANTHRANILATE-atom9" elementType="O" x2="-26517.0" y2="-13087.0" formalCharge="-1"/> <atom id="ANTHRANILATE-atom10" elementType="O" x2="-19372.0" y2="-25462.0"/> </atomArray> <bondArray> <bond id="ANTHRANILATE-bond1" atomRefs="ANTHRANILATE-atom7 ANTHRANILATE-atom8" order="1"/> <bond id="ANTHRANILATE-bond2" atomRefs="ANTHRANILATE-atom6 ANTHRANILATE-atom9" order="1"/> <bond id="ANTHRANILATE-bond3" atomRefs="ANTHRANILATE-atom6 ANTHRANILATE-atom10" order="2"/> <bond id="ANTHRANILATE-bond4" atomRefs="ANTHRANILATE-atom5 ANTHRANILATE-atom6" order="1"/> <bond id="ANTHRANILATE-bond5" atomRefs="ANTHRANILATE-atom3 ANTHRANILATE-atom4" order="2"/> <bond id="ANTHRANILATE-bond6" atomRefs="ANTHRANILATE-atom2 ANTHRANILATE-atom3" order="1"/> <bond id="ANTHRANILATE-bond7" atomRefs="ANTHRANILATE-atom1 ANTHRANILATE-atom2" order="2"/> <bond id="ANTHRANILATE-bond8" atomRefs="ANTHRANILATE-atom5 ANTHRANILATE-atom1" order="1"/> <bond id="ANTHRANILATE-bond9" atomRefs="ANTHRANILATE-atom7 ANTHRANILATE-atom4" order="1"/> <bond id="ANTHRANILATE-bond10" atomRefs="ANTHRANILATE-atom7 ANTHRANILATE-atom5" order="2"/> </bondArray> <formula concise="C 7 H 6 N 1 O 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">136.13</float> <string title="smiles">C(C1(=C(C=CC=C1)N))(=O)[O-]</string> </molecule> </cml> anthranilic acid 2-aminobenzoic acid vitamin L1 o-aminobenzoic acid 2-aminobenzoate MetaCyc ANTHRANILATE CAS 118-92-3 LIGAND C00108 PubChem 227 1 385.031 5-phosphoribosyl 1-pyrophosphate CML <cml> <molecule id="PRPP" title="5-phosphoribosyl 1-pyrophosphate" dictRef="dictPRPP"> <atomArray> <atom id="PRPP-atom1" elementType="O" x2="8297.0" y2="-19352.0"/> <atom id="PRPP-atom2" elementType="O" x2="76053.0" y2="-8710.0"/> <atom id="PRPP-atom3" elementType="O" x2="59553.0" y2="-8757.0"/> <atom id="PRPP-atom4" elementType="O" x2="27808.0" y2="0.0"/> <atom id="PRPP-atom5" elementType="O" x2="45758.0" y2="0.0"/> <atom id="PRPP-atom6" elementType="O" x2="8315.0" y2="-2852.0" formalCharge="-1"/> <atom id="PRPP-atom7" elementType="O" x2="0.0" y2="-11079.0" formalCharge="-1"/> <atom id="PRPP-atom8" elementType="O" x2="84303.0" y2="-17125.0" formalCharge="-1"/> <atom id="PRPP-atom9" elementType="O" x2="76153.0" y2="-25210.0" formalCharge="-1"/> <atom id="PRPP-atom10" elementType="O" x2="59553.0" y2="-25257.0" formalCharge="-1"/> <atom id="PRPP-atom11" elementType="C" x2="22263.0" y2="-17072.0"/> <atom id="PRPP-atom12" elementType="O" x2="16500.0" y2="-11167.0"/> <atom id="PRPP-atom13" elementType="O" x2="36783.0" y2="-19370.0"/> <atom id="PRPP-atom14" elementType="O" x2="51303.0" y2="-17072.0"/> <atom id="PRPP-atom15" elementType="O" x2="67803.0" y2="-16942.0"/> <atom id="PRPP-atom16" elementType="C" x2="32658.0" y2="-6677.0"/> <atom id="PRPP-atom17" elementType="C" x2="40908.0" y2="-6677.0"/> <atom id="PRPP-atom18" elementType="C" x2="30107.0" y2="-14520.0"/> <atom id="PRPP-atom19" elementType="C" x2="43454.0" y2="-14520.0"/> <atom id="PRPP-atom20" elementType="P" x2="8250.0" y2="-11102.0"/> <atom id="PRPP-atom21" elementType="P" x2="76053.0" y2="-16960.0"/> <atom id="PRPP-atom22" elementType="P" x2="59553.0" y2="-17007.0"/> </atomArray> <bondArray> <bond id="PRPP-bond1" atomRefs="PRPP-atom17 PRPP-atom19" order="1"/> <bond id="PRPP-bond2" atomRefs="PRPP-atom16 PRPP-atom18" order="1"/> <bond id="PRPP-bond3" atomRefs="PRPP-atom16 PRPP-atom17" order="1"/> <bond id="PRPP-bond4" atomRefs="PRPP-atom15 PRPP-atom22" order="1"/> <bond id="PRPP-bond5" atomRefs="PRPP-atom15 PRPP-atom21" order="1"/> <bond id="PRPP-bond6" atomRefs="PRPP-atom14 PRPP-atom22" order="1"/> <bond id="PRPP-bond7" atomRefs="PRPP-atom19 PRPP-atom14" order="1"/> <bond id="PRPP-bond8" atomRefs="PRPP-atom13 PRPP-atom19" order="1"/> <bond id="PRPP-bond9" atomRefs="PRPP-atom13 PRPP-atom18" order="1"/> <bond id="PRPP-bond10" atomRefs="PRPP-atom12 PRPP-atom20" order="1"/> <bond id="PRPP-bond11" atomRefs="PRPP-atom18 PRPP-atom11" order="1"/> <bond id="PRPP-bond12" atomRefs="PRPP-atom11 PRPP-atom12" order="1"/> <bond id="PRPP-bond13" atomRefs="PRPP-atom10 PRPP-atom22" order="1"/> <bond id="PRPP-bond14" atomRefs="PRPP-atom9 PRPP-atom21" order="1"/> <bond id="PRPP-bond15" atomRefs="PRPP-atom8 PRPP-atom21" order="1"/> <bond id="PRPP-bond16" atomRefs="PRPP-atom7 PRPP-atom20" order="1"/> <bond id="PRPP-bond17" atomRefs="PRPP-atom6 PRPP-atom20" order="1"/> <bond id="PRPP-bond18" atomRefs="PRPP-atom17 PRPP-atom5" order="1"/> <bond id="PRPP-bond19" atomRefs="PRPP-atom16 PRPP-atom4" order="1"/> <bond id="PRPP-bond20" atomRefs="PRPP-atom3 PRPP-atom22" order="2"/> <bond id="PRPP-bond21" atomRefs="PRPP-atom2 PRPP-atom21" order="2"/> <bond id="PRPP-bond22" atomRefs="PRPP-atom1 PRPP-atom20" order="2"/> </bondArray> <formula concise="C 5 H 8 O 14 P 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">385.031</float> <string title="smiles">C(OP(=O)([O-])[O-])C1(OC(OP(=O)([O-])OP(=O)([O-])[O-])C(O)C(O)1)</string> </molecule> </cml> PRPP 5-phospho-&alpha;-D-ribose 1-diphosphate 5-phosphoribosyl diphosphate 5-phosphoribosyl-1-PP 5-phosphoribosyl-PP 5-phosphoribosyl-1-pyrophosphate 5-phosphoribosylpyrophosphate phosphoribosylpyrophosphate 5-phospho-ribosyl-pyrophosphate &alpha;-D-5-phosphoribosylPP &alpha;-D-5-P-RibosylPP 5-phospho-&alpha;-D-ribose-1-diphosphate MetaCyc PRPP CAS 13270-65-0 LIGAND C00119 1 Phosphoribosyl-anthranilate diphosphorylase Phosphoribosyl-anthranilate pyrophosphorylase anthranilate phosphoribosyltransfer PR transferase MetaCyc PRTRANS-RXN UniProt P94326 UniProt Q9ZFA8 UniProt Q9S592 UniProt O68608 UniProt Q43085 UniProt O49435 UniProt Q9T0C8 UniProt O65279 UniProt O80558 UniProt P73617 UniProt Q02000 UniProt P30525 UniProt P26924 UniProt P00500 UniProt P07285 UniProt P03947 UniProt P00904 RELATED-TO UniProt P00905 RELATED-TO UniProt P00906 RELATED-TO UniProt P17170 UniProt P18261 UniProt P56737 UniProt P43858 UniProt P06559 UniProt Q08654 RELATED-TO UniProt P20575 UniProt P20574 UniProt P66995 UniProt P42392 UniProt P12321 UniProt P12320 Component II has two enzymatic activities. It provides the amidotransferase activity in the anthranilate synthase reaction in conjunction with component I. On its own it catalyzes the anthranilate phosphoribosyltransferase reaction, which is the second reaction in the tryptophan biosynthetic pathway. anthranilate synthase component II TrpGD anthranilate phosphoribosyltransferase MetaCyc MONOMER-282 UniProt Q08654 Swiss-Model Q08654 ModBase Q08654 2 CPLX-1782 MetaCyc CPLX-1782 1 REVERSIBLE anthranilate phosphoribosyltransferase phosphoribosyl-anthranilate pyrophosphorylase <I>N</I>-(5-phospho-D-ribosyl)-anthranilate:pyrophosphate phospho-&alpha;-D-ribosyltransferase MetaCyc ENZRXN-2602 Kim CW Markiewicz P Lee JJ Schierle CF Miller JH PubMed 7685830 J Mol Biol 1993;231(4);960-81 Studies of the hyperthermophile Thermotoga maritima by random sequencing of cDNA and genomic libraries. Identification and sequencing of the trpEG (D) operon. 1993 Tryptophan is a competitive inhibitor with respect to 5-phosphoribosyl 1-pyrophosphate. The Ki for this inhibition is 0.5 &micro;M |CITS: [2429387]|. Anthranilate phosphoribosyl transferase (TrpD) catalyzes the second step in the pathway of tryptophan biosynthesis. TrpD catalyzes a phosphoribosyltransferase reaction that generates N-(5'-phosphoribosyl)-anthranilate |CITS: [2428387]|. The phosphoribosyl transferase and anthranilate synthase contributing portions of TrpD are present in different portions of the protein. The anthranilate synthase reaction requires the amino-terminal portion of the protein, whereas the phosphoribosyltransferase reaction requires the carboxy-terminal region |CITS: [4590474]|. anthranilate synthase component II B1263 TrpD TrpGD MetaCyc ANTHRANSYNCOMPII-MONOMER UniProt P00904 RefSeq NP_415779 Pfam PF00117 IN-FAMILY Swiss-Model P00904 ModBase P00904 EcoliWiki b1263 1 anthranilate phosphoribosyl transferase N-(5-phospho-D-ribosyl)-anthranilate:pyrophosphate phospho-&alpha;-D-ribosyltransferase phosphoribosyl-anthranilate pyrophosphorylase MetaCyc ENZRXN0-6543 Anthranilate synthase is composed of two components. Component I, the trpE gene product, can catalyze the formation of anthranilate using ammonia rather than glutamine. Component II, the trpGD gene product, provides the amidotransferase activity. 4.1.3.27 1 146.146 L-glutamine CML <cml> <molecule id="GLN" title="L-glutamine" dictRef="dictGLN"> <atomArray> <atom id="GLN-atom1" elementType="C" x2="1410.0" y2="1032.0"/> <atom id="GLN-atom2" elementType="C" x2="1480.0" y2="988.0"/> <atom id="GLN-atom3" elementType="C" x2="1337.0" y2="993.0"/> <atom id="GLN-atom4" elementType="N" x2="1412.0" y2="1115.0" formalCharge="1"/> <atom id="GLN-atom5" elementType="C" x2="1553.0" y2="1027.0"/> <atom id="GLN-atom6" elementType="O" x2="1268.0" y2="1040.0" formalCharge="-1"/> <atom id="GLN-atom7" elementType="O" x2="1338.0" y2="911.0"/> <atom id="GLN-atom8" elementType="C" x2="1623.0" y2="984.0"/> <atom id="GLN-atom9" elementType="N" x2="1695.0" y2="1023.0"/> <atom id="GLN-atom10" elementType="O" x2="1624.0" y2="901.0"/> </atomArray> <bondArray> <bond id="GLN-bond1" atomRefs="GLN-atom1 GLN-atom2" order="1"/> <bond id="GLN-bond2" atomRefs="GLN-atom1 GLN-atom3" order="1"/> <bond id="GLN-bond3" atomRefs="GLN-atom4 GLN-atom1" order="1"/> <bond id="GLN-bond4" atomRefs="GLN-atom2 GLN-atom5" order="1"/> <bond id="GLN-bond5" atomRefs="GLN-atom3 GLN-atom6" order="1"/> <bond id="GLN-bond6" atomRefs="GLN-atom3 GLN-atom7" order="2"/> <bond id="GLN-bond7" atomRefs="GLN-atom5 GLN-atom8" order="1"/> <bond id="GLN-bond8" atomRefs="GLN-atom8 GLN-atom9" order="1"/> <bond id="GLN-bond9" atomRefs="GLN-atom8 GLN-atom10" order="2"/> </bondArray> <formula concise="C 5 H 10 N 2 O 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">146.146</float> <string title="smiles">C(=O)([O-])C([N+])CCC(=O)N</string> </molecule> </cml> Q proglumide glum gln glutamine glumin 2-aminoglutaramic acid glutamic acid 5-amide MetaCyc GLN CAS 56-85-9 LIGAND C00064 1 Anthranilate synthase 1 1 146.122 L-glutamate CML <cml> <molecule id="GLT" title="L-glutamate" dictRef="dictGLT"> <atomArray> <atom id="GLT-atom1" elementType="C" x2="1405.0" y2="1029.0"/> <atom id="GLT-atom2" elementType="C" x2="1475.0" y2="985.0"/> <atom id="GLT-atom3" elementType="C" x2="1333.0" y2="990.0"/> <atom id="GLT-atom4" elementType="N" x2="1407.0" y2="1111.0" formalCharge="1"/> <atom id="GLT-atom5" elementType="C" x2="1548.0" y2="1024.0"/> <atom id="GLT-atom6" elementType="O" x2="1263.0" y2="1037.0" formalCharge="-1"/> <atom id="GLT-atom7" elementType="O" x2="1334.0" y2="908.0"/> <atom id="GLT-atom8" elementType="C" x2="1618.0" y2="981.0"/> <atom id="GLT-atom9" elementType="O" x2="1690.0" y2="1020.0" formalCharge="-1"/> <atom id="GLT-atom10" elementType="O" x2="1619.0" y2="898.0"/> </atomArray> <bondArray> <bond id="GLT-bond1" atomRefs="GLT-atom1 GLT-atom2" order="1"/> <bond id="GLT-bond2" atomRefs="GLT-atom1 GLT-atom3" order="1"/> <bond id="GLT-bond3" atomRefs="GLT-atom1 GLT-atom4" order="1"/> <bond id="GLT-bond4" atomRefs="GLT-atom2 GLT-atom5" order="1"/> <bond id="GLT-bond5" atomRefs="GLT-atom3 GLT-atom6" order="1"/> <bond id="GLT-bond6" atomRefs="GLT-atom3 GLT-atom7" order="2"/> <bond id="GLT-bond7" atomRefs="GLT-atom5 GLT-atom8" order="1"/> <bond id="GLT-bond8" atomRefs="GLT-atom8 GLT-atom9" order="1"/> <bond id="GLT-bond9" atomRefs="GLT-atom8 GLT-atom10" order="2"/> </bondArray> <formula concise="C 5 H 8 N 1 O 4" formalCharge="0"/> <float title="molecularWeight" units="g/mol">146.122</float> <string title="smiles">C(=O)([O-])C([N+])CCC(=O)[O-]</string> </molecule> </cml> L-Glutamate 1-amino-propane-1,3-dicarboxylic acid glutacid glutaminic acid L-glutamic acid &alpha;-aminoglutaric acid E glt glu glut glutamate L-glu 2-aminopentanedioic acid MetaCyc GLT CAS 56-86-0 LIGAND C00025 1 87.055 pyruvate CML <cml> <molecule id="PYRUVATE" title="pyruvate" dictRef="dictPYRUVATE"> <atomArray> <atom id="PYRUVATE-atom1" elementType="C" x2="3921.0" y2="-2553.0"/> <atom id="PYRUVATE-atom2" elementType="C" x2="-10803.0" y2="-2997.0"/> <atom id="PYRUVATE-atom3" elementType="O" x2="-3700.0" y2="9434.0"/> <atom id="PYRUVATE-atom4" elementType="C" x2="-3700.0" y2="1184.0"/> <atom id="PYRUVATE-atom5" elementType="O" x2="3921.0" y2="-10803.0"/> <atom id="PYRUVATE-atom6" elementType="O" x2="10766.0" y2="2035.0" formalCharge="-1"/> </atomArray> <bondArray> <bond id="PYRUVATE-bond1" atomRefs="PYRUVATE-atom6 PYRUVATE-atom1" order="1"/> <bond id="PYRUVATE-bond2" atomRefs="PYRUVATE-atom5 PYRUVATE-atom1" order="2"/> <bond id="PYRUVATE-bond3" atomRefs="PYRUVATE-atom4 PYRUVATE-atom1" order="1"/> <bond id="PYRUVATE-bond4" atomRefs="PYRUVATE-atom3 PYRUVATE-atom4" order="2"/> <bond id="PYRUVATE-bond5" atomRefs="PYRUVATE-atom2 PYRUVATE-atom4" order="1"/> </bondArray> <formula concise="C 3 H 3 O 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">87.055</float> <string title="smiles">C(C(C)=O)(=O)[O-]</string> </molecule> </cml> alpha-ketopropionic acid BTS &alpha;-ketopropionic acid acetylformic acid pyroracemic acid 2-oxopropanoic acid pyruvic acid 2-oxopropanoate 2-oxo-propionic acid MetaCyc PYRUVATE UMBBD-Compounds c0159 CAS 127-17-3 LIGAND C00022 LIGAND c00022 1 anthranilate synthesis MetaCyc ANTHRANSYN-RXN UniProt Q41156 RELATED-TO UniProt Q9ZFA9 UniProt Q9RQG2 UniProt Q9X7C5 UniProt Q9S593 UniProt Q92370 RELATED-TO UniProt P48261 UniProt Q08073 UniProt O81533 UniProt P74130 UniProt P20170 UniProt Q55144 UniProt P51362 UniProt Q02003 UniProt P24773 RELATED-TO UniProt P32069 UniProt P30526 UniProt P25170 RELATED-TO UniProt P23315 UniProt P06531 RELATED-TO UniProt P05328 RELATED-TO UniProt P14952 UniProt P00900 UniProt P00901 UniProt P00908 RELATED-TO UniProt P00902 UniProt P00904 RELATED-TO UniProt P00895 RELATED-TO UniProt P00905 RELATED-TO UniProt P00906 RELATED-TO UniProt P00898 UniProt P00896 UniProt P00937 RELATED-TO UniProt P00899 UniProt P03963 UniProt P14953 UniProt P20409 RELATED-TO UniProt Q42565 UniProt P32068 UniProt P18267 UniProt Q06128 RELATED-TO UniProt P42388 UniProt P42387 UniProt Q9PIF5 UniProt Q9XAZ0 UniProt Q57690 UniProt Q02001 UniProt Q9JUS0 UniProt P09785 UniProt P20579 UniProt Q8X3T1 UniProt Q08653 RELATED-TO UniProt P20580 UniProt Q8X3T2 UniProt Q08654 RELATED-TO UniProt Q57686 UniProt P43761 UniProt P20441 UniProt Q58475 UniProt Q9R5Z6 UniProt P33974 UniProt Q06129 RELATED-TO UniProt P09786 UniProt P20463 UniProt P06557 UniProt Q9PIF4 UniProt P33975 UniProt P21690 UniProt P15395 UniProt P00897 2 Component I can catalyze the formation of anthranilate using ammonia rather than glutamine. Component II provides the amidotransferase activity. anthranilate synthase component I TrpE MetaCyc MONOMER-281 UniProt Q08653 Swiss-Model Q08653 ModBase Q08653 2 CPLX-1781 MetaCyc CPLX-1781 1 REVERSIBLE anthranilate synthase chorismate pyruvate-lyase MetaCyc ENZRXN-2601 anthranilate synthase beta subunit TrpG anthranilate synthase component II MetaCyc MONOMER-3604 UniProt Q06129 Swiss-Model Q06129 ModBase Q06129 Tutino ML Tosco A Marino G Sannia G PubMed 9016772 Biochem Biophys Res Commun 230(2);306-10 Expression of Sulfolobus solfataricus trpE and trpG genes in E. coli. 1997 2 anthranilate synthase alpha subunit TrpE anthranilate synthase component I MetaCyc MONOMER-3603 UniProt Q06128 Swiss-Model Q06128 ModBase Q06128 2 CPLX-2981 anthranilate synthase MetaCyc CPLX-2981 1 anthranilate synthase MetaCyc ENZRXN-3703 A cDNA clone was isolated from the common rue and shown to encode the functional anthranilate synthase alpha 1 enzyme by complementation in E.coli deletion mutants, defective for anthranilate synthase. Its transcription corresponds to elicitor induced alkaloid accumulation |CITS: [7757119]|. MONOMER-14029 Ruta graveolens NCBI Taxonomy 37565 anthranilate synthase alpha subunit MetaCyc MONOMER-14029 Entrez AAA74900 UniProt Q41155 1 alpha1 anthranilate synthase MetaCyc ENZRXN-15062 A cDNA clone was isolated from the common rue and shown to encode one of the anthranilate synthase genes AS &alpha;2. This enzyme is constitutively expressed and not elicitor induced |CITS: [7757119]|. MONOMER-14031 anthranilate synthase alpha subunit MetaCyc MONOMER-14031 Entrez AAA74901 UniProt Q41156 1 alpha2 anthranilate synthase MetaCyc ENZRXN-15064 1 Both tryptophan and 7-methyltryptophan are competitive inhibitors with respect to chorismate |CITS: [5333199][4904235]|. Anthranilate synthase (TrpDE) catalyzes the first step in the pathway of tryptophan biosynthesis, and is subject to feedback regulation by the end product of the pathway. One of its component monomers also catalyzes the second step in the same pathway. TrpDE catalyzes the glutamine amidotransferase reaction that adds an amine group from glutamine to chorismate to yield anthranilate and glutamate |CITS: [5333199][4886289]|. TrpE on its own can carry out an alternate version of this reaction, using ammonium sulfate rather than glutamine as an amino donor |CITS: [4886289]|. TrpD dramatically increases the affinity of TrpE for glutamine over TrpE alone |CITS: [4886290]|. TrpDE functions as a as complex comprising two TrpD and two TrpE monomers |CITS: [4598537]|. In line with their role in synthesizing tryptophan, the components of this complex contain almost no tryptophan, with one residue in TrpD and none in TrpE |CITS: [7021857]|. Translation of TrpE and TrpD is coordinated via a specialized intercistronic sequence between <i>trpE</i> and <i>trpD</i>. If the latter portion of the <i>trpE</i> mRNA is not translated, <i>trpD</i> mRNA translation is markedly reduced |CITS: [7021857]|. 2 anthranilate synthase component I B1264 TryD TrpE &alpha; subunit MetaCyc ANTHRANSYNCOMPI-MONOMER UniProt P00895 RefSeq NP_415780 Pfam PF04715 IN-FAMILY Swiss-Model P00895 ModBase P00895 EcoliWiki b1264 2 ANTHRANSYN-CPLX MetaCyc ANTHRANSYN-CPLX 1 anthranilate synthase ASase MetaCyc ANTHRANSYN-ENZRXN 1 RXN0-2381 117.15 indole CML <cml> <molecule id="INDOLE" title="indole" dictRef="dictINDOLE"> <atomArray> <atom id="INDOLE-atom1" elementType="C" x2="-9829.0" y2="-15217.0"/> <atom id="INDOLE-atom2" elementType="C" x2="-16973.0" y2="-11092.0"/> <atom id="INDOLE-atom3" elementType="C" x2="-16973.0" y2="-2842.0"/> <atom id="INDOLE-atom4" elementType="C" x2="-9829.0" y2="1283.0"/> <atom id="INDOLE-atom5" elementType="C" x2="-2684.0" y2="-2842.0"/> <atom id="INDOLE-atom6" elementType="C" x2="-2684.0" y2="-11092.0"/> <atom id="INDOLE-atom7" elementType="N" x2="4460.0" y2="1283.0"/> <atom id="INDOLE-atom8" elementType="C" x2="11605.0" y2="-11092.0"/> <atom id="INDOLE-atom9" elementType="C" x2="11605.0" y2="-2842.0"/> </atomArray> <bondArray> <bond id="INDOLE-bond1" atomRefs="INDOLE-atom1 INDOLE-atom2" order="2"/> <bond id="INDOLE-bond2" atomRefs="INDOLE-atom2 INDOLE-atom3" order="1"/> <bond id="INDOLE-bond3" atomRefs="INDOLE-atom3 INDOLE-atom4" order="2"/> <bond id="INDOLE-bond4" atomRefs="INDOLE-atom4 INDOLE-atom5" order="1"/> <bond id="INDOLE-bond5" atomRefs="INDOLE-atom1 INDOLE-atom6" order="1"/> <bond id="INDOLE-bond6" atomRefs="INDOLE-atom6 INDOLE-atom8" order="1"/> <bond id="INDOLE-bond7" atomRefs="INDOLE-atom5 INDOLE-atom6" order="2"/> <bond id="INDOLE-bond8" atomRefs="INDOLE-atom7 INDOLE-atom5" order="1"/> <bond id="INDOLE-bond9" atomRefs="INDOLE-atom8 INDOLE-atom9" order="2"/> <bond id="INDOLE-bond10" atomRefs="INDOLE-atom7 INDOLE-atom9" order="1"/> </bondArray> <formula concise="C 8 H 7 N 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">117.15</float> <string title="smiles">C1(NC2(=C(C=1)C=CC=C2))</string> </molecule> </cml> MetaCyc INDOLE CAS 120-72-9 LIGAND C00463 1 168.043 D-glyceraldehyde-3-phosphate CML <cml> <molecule id="GAP" title="D-glyceraldehyde-3-phosphate" dictRef="dictGAP"> <atomArray> <atom id="GAP-atom1" elementType="O" x2="0.0" y2="-3237500.0"/> <atom id="GAP-atom2" elementType="O" x2="2991500.0" y2="-781200.0"/> <atom id="GAP-atom3" elementType="O" x2="716000.0" y2="-2827500.0"/> <atom id="GAP-atom4" elementType="O" x2="2210600.0" y2="0.0" formalCharge="-1"/> <atom id="GAP-atom5" elementType="O" x2="2210600.0" y2="-1562200.0" formalCharge="-1"/> <atom id="GAP-atom6" elementType="C" x2="2900.0" y2="-2412500.0"/> <atom id="GAP-atom7" elementType="C" x2="721800.0" y2="-1177400.0"/> <atom id="GAP-atom8" elementType="O" x2="1445500.0" y2="-781200.0"/> <atom id="GAP-atom9" elementType="C" x2="718900.0" y2="-2002400.0"/> <atom id="GAP-atom10" elementType="P" x2="2210600.0" y2="-781200.0"/> </atomArray> <bondArray> <bond id="GAP-bond1" atomRefs="GAP-atom8 GAP-atom10" order="1"/> <bond id="GAP-bond2" atomRefs="GAP-atom7 GAP-atom9" order="1"/> <bond id="GAP-bond3" atomRefs="GAP-atom7 GAP-atom8" order="1"/> <bond id="GAP-bond4" atomRefs="GAP-atom6 GAP-atom9" order="1"/> <bond id="GAP-bond5" atomRefs="GAP-atom5 GAP-atom10" order="1"/> <bond id="GAP-bond6" atomRefs="GAP-atom4 GAP-atom10" order="1"/> <bond id="GAP-bond7" atomRefs="GAP-atom9 GAP-atom3" order="1"/> <bond id="GAP-bond8" atomRefs="GAP-atom2 GAP-atom10" order="2"/> <bond id="GAP-bond9" atomRefs="GAP-atom1 GAP-atom6" order="2"/> </bondArray> <formula concise="C 3 H 5 O 6 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">168.043</float> <string title="smiles">C(=O)C(O)COP(=O)([O-])[O-]</string> </molecule> </cml> D-glyceraldehdye-3-phosphate 3-phosphoglyceraldehyde D-glyceraldehyde-3-P glyceraldehyde-3-phosphate gap glyceraldehyde-phosphate glyceraldehyde-P glyceraldehyde-3-P (2<i>R</i>)-2-hydroxy-3-(phosphonooxy)-propanal MetaCyc GAP CAS 142-10-9 LIGAND C00661 1 MetaCyc RXN0-2381 The alpha subunit carries out the aldol cleavage of indoleglycerol phosphate yielding indole and glyceraldehyde 3-phosphate. This subunit forms an &alpha;&beta;&beta;&alpha; complex in the native organism, where the indole is directly transferred through an internal tunnel to the beta subunit for further processing. However, it has been shown that <i>in vitro</i> it exists as a monomer which retains its catalytic properties. alpha subunit of tryptophan synthase TrpA &alpha; chain MetaCyc MONOMER-344 UniProt P50908 Swiss-Model P50908 ModBase P50908 Hettwer S Sterner R PubMed 11756459 J Biol Chem 277(10);8194-201 A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role. 2002 1 REVERSIBLE ENZRXN-3666 MetaCyc ENZRXN-3666 tryptophan synthase subunit alpha TrpA tk-TrpA MetaCyc MONOMER-3561 UniProt Q9YGA9 Swiss-Model Q9YGA9 ModBase Q9YGA9 1 ENZRXN-3667 MetaCyc ENZRXN-3667 The TrpA polypeptide (TSase &alpha;) functions as the &alpha; subunit of the tetrameric (&alpha;2-&beta;2) tryptophan synthase complex. As a purified protein, the &alpha; subunit is a monomer. TSase &alpha; contains the binding site for indole-3-glycerol-phosphate (InGP) and can carry out the cleavage reaction of InGP to indole and glyceraldehyde-3-phosphate, also termed the alpha reaction. Within the physiological complex with the &beta; subunit, the reaction rate is increased by 1-2 orders of magnitude. The reaction carried out by the &alpha; subunit alone is reversible, while the overall reaction is not. Crystal structures of the wild-type and a double mutant TrpA protein have been reported at 2.5 and 1.8 &Aring; resolution, respectively |CITS: [14684907][15879705]|. tryptophan synthase, alpha subunit B1260 Try TrpA &alpha; subunit TSase &alpha; MetaCyc TRYPSYN-APROTEIN Pfam PF00290 IN-FAMILY UniProt P0A877 ModBase P0A877 PDB 1XCF PDB 1XC4 PDB 1WQ5 PDB 1V7Y RefSeq NP_415776 EcoliWiki b1260 1 indoleglycerol phosphate aldolase MetaCyc ENZRXN0-3381 4.2.1.20 1 105.093 L-serine CML <cml> <molecule id="SER" title="L-serine" dictRef="dictSER"> <atomArray> <atom id="SER-atom1" elementType="C" x2="1399.0" y2="1039.0"/> <atom id="SER-atom2" elementType="C" x2="1329.0" y2="995.0"/> <atom id="SER-atom3" elementType="C" x2="1470.0" y2="998.0"/> <atom id="SER-atom4" elementType="N" x2="1401.0" y2="1122.0" formalCharge="1"/> <atom id="SER-atom5" elementType="O" x2="1257.0" y2="1035.0" formalCharge="-1"/> <atom id="SER-atom6" elementType="O" x2="1331.0" y2="912.0"/> <atom id="SER-atom7" elementType="O" x2="1543.0" y2="1041.0"/> </atomArray> <bondArray> <bond id="SER-bond1" atomRefs="SER-atom1 SER-atom2" order="1"/> <bond id="SER-bond2" atomRefs="SER-atom1 SER-atom3" order="1"/> <bond id="SER-bond3" atomRefs="SER-atom4 SER-atom1" order="1"/> <bond id="SER-bond4" atomRefs="SER-atom2 SER-atom5" order="1"/> <bond id="SER-bond5" atomRefs="SER-atom2 SER-atom6" order="2"/> <bond id="SER-bond6" atomRefs="SER-atom3 SER-atom7" order="1"/> </bondArray> <formula concise="C 3 H 7 N 1 O 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">105.093</float> <string title="smiles">C(=O)([O-])C([N+])CO</string> </molecule> </cml> S serine ser L-ser MetaCyc SER CAS 56-45-1 LIGAND C00065 LIGAND C00065 1 RXN0-2382 204.228 L-tryptophan CML <cml> <molecule id="TRP" title="L-tryptophan" dictRef="dictTRP"> <atomArray> <atom id="TRP-atom1" elementType="N" x2="4093.0" y2="-3306.0" formalCharge="1"/> <atom id="TRP-atom2" elementType="O" x2="2629.0" y2="-4061.0"/> <atom id="TRP-atom3" elementType="O" x2="1894.0" y2="-2818.0" formalCharge="-1"/> <atom id="TRP-atom4" elementType="C" x2="0.0" y2="-1692.0"/> <atom id="TRP-atom5" elementType="C" x2="0.0" y2="-892.0"/> <atom id="TRP-atom6" elementType="C" x2="696.0" y2="-2128.0"/> <atom id="TRP-atom7" elementType="C" x2="696.0" y2="-449.0"/> <atom id="TRP-atom8" elementType="C" x2="2648.0" y2="-944.0"/> <atom id="TRP-atom9" elementType="C" x2="3377.0" y2="-2043.0"/> <atom id="TRP-atom10" elementType="C" x2="2629.0" y2="-3215.0"/> <atom id="TRP-atom11" elementType="C" x2="2648.0" y2="-1653.0"/> <atom id="TRP-atom12" elementType="C" x2="1451.0" y2="-1653.0"/> <atom id="TRP-atom13" elementType="C" x2="1451.0" y2="-944.0"/> <atom id="TRP-atom14" elementType="C" x2="3377.0" y2="-2857.0"/> <atom id="TRP-atom15" elementType="N" x2="2050.0" y2="-514.0"/> </atomArray> <bondArray> <bond id="TRP-bond1" atomRefs="TRP-atom14 TRP-atom1" order="1"/> <bond id="TRP-bond2" atomRefs="TRP-atom2 TRP-atom10" order="2"/> <bond id="TRP-bond3" atomRefs="TRP-atom3 TRP-atom10" order="1"/> <bond id="TRP-bond4" atomRefs="TRP-atom4 TRP-atom5" order="2"/> <bond id="TRP-bond5" atomRefs="TRP-atom6 TRP-atom4" order="1"/> <bond id="TRP-bond6" atomRefs="TRP-atom5 TRP-atom7" order="1"/> <bond id="TRP-bond7" atomRefs="TRP-atom12 TRP-atom6" order="2"/> <bond id="TRP-bond8" atomRefs="TRP-atom7 TRP-atom13" order="2"/> <bond id="TRP-bond9" atomRefs="TRP-atom11 TRP-atom8" order="2"/> <bond id="TRP-bond10" atomRefs="TRP-atom8 TRP-atom15" order="1"/> <bond id="TRP-bond11" atomRefs="TRP-atom9 TRP-atom11" order="1"/> <bond id="TRP-bond12" atomRefs="TRP-atom14 TRP-atom9" order="1"/> <bond id="TRP-bond13" atomRefs="TRP-atom10 TRP-atom14" order="1"/> <bond id="TRP-bond14" atomRefs="TRP-atom12 TRP-atom11" order="1"/> <bond id="TRP-bond15" atomRefs="TRP-atom13 TRP-atom12" order="1"/> <bond id="TRP-bond16" atomRefs="TRP-atom15 TRP-atom13" order="1"/> </bondArray> <formula concise="C 11 H 12 N 2 O 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">204.228</float> <string title="smiles">C1(NC2(C(C(CC(C([O-])=O)[N+])=1)=CC=CC=2))</string> </molecule> </cml> trp W tryptacin trofan tryptophan 2-amino-3-indolylpropanic acid MetaCyc TRP CAS 73-22-3 LIGAND C00078 CAS 6912-86-3 1 1 MetaCyc RXN0-2382 While this homodimer protein is able to catalyze the reaction on its own, in the cell it combines with the alpha subunit to form a protein complex with the structure &alpha;&beta;&beta;&alpha;. Size estimation of the tryptophan synthase beta1 protein by gel filtration resulted in a mass of 49.4 KDa, which is in between the calculated molecular masses for the monomer and dimer, which are 42.9 and 85.8 KDa, resepectively. Analytical ultra-centrifugation (sedimentation equilibrium) showed the protein's mass to be 91 KDa, confirming it exists as a homodimer |CITS: [11756459]|. The beta1 subunit is part of the tryptophan synthase complex, and catalyzes the synthesis of tryptophan from indole and L-serine. This subunit forms an &alpha;&beta;&beta;&alpha; complex in the native organism, where the indole, which is the product of the alpha subunit, is directly transferred through an internal tunnel to the beta subunit. However, it has been shown that <i>in vitro</i> it forms a homodimer, that catalyzes the same reaction. beta subunit of tryptophan synthase TrpB &beta; chain MetaCyc MONOMER-345 UniProt P50909 Swiss-Model P50909 ModBase P50909 2 tryptophan synthase beta1 dimer tryptophan synthase &beta; dimer MetaCyc CPLX-2945 1 tryptophan synthase beta1 dimer MetaCyc ENZRXN-3664 Most mesophilic bacteria have a tryptophan synthase complex, which is made of two &alpha; subunits and two &beta; subunits, with the composition &alpha;&beta;&beta;&alpha;. The &alpha; subunits catalyze the conversion of indole 3 glycerol phosphate to indole, which is hydrophobic. The indole is transferred in an internal tunnel to the &beta; units, which convert it to tryptophan. This process is very efficient at 37 degrees. However, at the high temperatures in which hyperthermophilic organisms live accelerated diffusion may cause loss of indole. These organisms have a second version of the &beta; subunit, termed B2, which forms a homodimer, but does not combine with the &alpha; unit to form a multi complex. This homodimer also catalyzes the conversion of indole to tryptophan, but has a much lower Km for indole. It has been suggested that the role of this enzyme is to scavenge the liberated indole and prevent it from penetrating through the cytoplasmic membrane |CITS: [11756459]|. Size estimation of the tryptophan synthase beta2 protein by gel filtration resulted in a mass of 61.7 KDa, which is in between the calculated molecular masses for the monomer and dimer, which are 46.4 and 92.8 KDa, resepectively. Analytical ultra-centrifugation (sedimentation equilibrium) showed the protein's mass to be 98 KDa, confirming it exists as a homodimer |CITS: [11756459]|. Most mesophilic bacteria have a tryptophan synthase complex, which is made of two &alpha; subunits and two &beta; subunits, with the composition &alpha;&beta;&beta;&alpha;. The &alpha; subunits catalyze the conversion of indole 3 glycerol phosphate to indole, which is hydrophobic. The indole is transferred in an internal tunnel to the &beta; units, which convert it to tryptophan. This process is very efficient at 37 degrees. However, at the high temperatures in which hyperthermophilic organisms live accelerated diffusion may cause loss of indole. These organisms have a second version of the &beta; subunit, termed B2, which forms a homodimer, but does not combine with the &alpha; unit to form a multi complex. This homodimer also catalyzes the conversion of indole to tryptophan, but has a much lower Km for indole. It has been suggested that the role of this enzyme is to scavenge the liberated indole and prevent it from penetrating through the cytoplasmic membrane |CITS: [11756459]| tryptophan synthase beta2 subunit TrpB2 Trp &beta;2 tmTrpB2 MetaCyc MONOMER-3543 UniProt Q9WZ09 Swiss-Model Q9WZ09 ModBase Q9WZ09 2 CPLX-2946 MetaCyc CPLX-2946 1 tryptophan synthase beta2 dimer MetaCyc ENZRXN-3665 tryptophan synthase beta subunit TrpB MetaCyc MONOMER-3562 UniProt Q9YGB0 Swiss-Model Q9YGB0 ModBase Q9YGB0 Tang XF Ezaki S Atomi H Imanaka T PubMed 11029579 Eur J Biochem 267(21);6369-77 Biochemical analysis of a thermostable tryptophan synthase from a hyperthermophilic archaeon. 2000 2 tryptophan synthase beta subunit dimer MetaCyc CPLX-2961 1 tryptophan synthase beta subunit dimer MetaCyc ENZRXN-3682 The TrpB polypeptide functions as the &beta; subunit of the tetrameric (&alpha;2-&beta;2) tryptophan synthase complex. The TrpB protein forms a homodimer (TSase &beta;2) in which each subunit contains a molecule of the cofactor pyridoxal phosphate covalently linked to the epsilon-amino group of a lysine residue via a Schiff base |CITS: [788781]|. This complex catalyzes the synthesis of L-tryptophan from indole and L-serine, also termed the beta reaction. This partial reaction carried out by the beta complex is irreversible. The TrpB subunit possesses binding sites for L-serine and PLP and can catalyze a variety of reactions involving these compounds. tryptophan synthase, beta subunit B1261 TrpB &beta; subunit MetaCyc TRYPSYN-BPROTEIN RefSeq NP_415777 UniProt P0A879 Pfam PF00291 IN-FAMILY Swiss-Model P0A879 ModBase P0A879 EcoliWiki b1261 2 tryptophan synthase, beta subunit dimer TSase &beta;2 MetaCyc CPLX0-2401 1 ENZRXN0-3701 MetaCyc ENZRXN0-3701 2.6.1.57 163.152 phenylpyruvate CML <cml> <molecule id="PHENYL-PYRUVATE" title="phenylpyruvate" dictRef="dictPHENYL-PYRUVATE"> <atomArray> <atom id="PHENYL-PYRUVATE-atom1" elementType="C" x2="-1692.0" y2="-387.0"/> <atom id="PHENYL-PYRUVATE-atom2" elementType="C" x2="-1692.0" y2="2357.0"/> <atom id="PHENYL-PYRUVATE-atom3" elementType="C" x2="-1692.0" y2="580.0"/> <atom id="PHENYL-PYRUVATE-atom4" elementType="O" x2="-1692.0" y2="-2370.0"/> <atom id="PHENYL-PYRUVATE-atom5" elementType="C" x2="-1076.0" y2="-1862.0"/> <atom id="PHENYL-PYRUVATE-atom6" elementType="C" x2="-1040.0" y2="1801.0"/> <atom id="PHENYL-PYRUVATE-atom7" elementType="O" x2="-435.0" y2="-423.0"/> <atom id="PHENYL-PYRUVATE-atom8" elementType="C" x2="-1076.0" y2="-907.0"/> <atom id="PHENYL-PYRUVATE-atom9" elementType="C" x2="-2370.0" y2="1052.0"/> <atom id="PHENYL-PYRUVATE-atom10" elementType="C" x2="-1076.0" y2="1052.0"/> <atom id="PHENYL-PYRUVATE-atom11" elementType="C" x2="-2370.0" y2="1801.0"/> <atom id="PHENYL-PYRUVATE-atom12" elementType="O" x2="-435.0" y2="-2309.0" formalCharge="-1"/> </atomArray> <bondArray> <bond id="PHENYL-PYRUVATE-bond1" atomRefs="PHENYL-PYRUVATE-atom11 PHENYL-PYRUVATE-atom9" order="2"/> <bond id="PHENYL-PYRUVATE-bond2" atomRefs="PHENYL-PYRUVATE-atom10 PHENYL-PYRUVATE-atom6" order="1"/> <bond id="PHENYL-PYRUVATE-bond3" atomRefs="PHENYL-PYRUVATE-atom9 PHENYL-PYRUVATE-atom3" order="1"/> <bond id="PHENYL-PYRUVATE-bond4" atomRefs="PHENYL-PYRUVATE-atom8 PHENYL-PYRUVATE-atom5" order="1"/> <bond id="PHENYL-PYRUVATE-bond5" atomRefs="PHENYL-PYRUVATE-atom8 PHENYL-PYRUVATE-atom7" order="2"/> <bond id="PHENYL-PYRUVATE-bond6" atomRefs="PHENYL-PYRUVATE-atom6 PHENYL-PYRUVATE-atom2" order="2"/> <bond id="PHENYL-PYRUVATE-bond7" atomRefs="PHENYL-PYRUVATE-atom5 PHENYL-PYRUVATE-atom12" order="1"/> <bond id="PHENYL-PYRUVATE-bond8" atomRefs="PHENYL-PYRUVATE-atom5 PHENYL-PYRUVATE-atom4" order="2"/> <bond id="PHENYL-PYRUVATE-bond9" atomRefs="PHENYL-PYRUVATE-atom3 PHENYL-PYRUVATE-atom1" order="1"/> <bond id="PHENYL-PYRUVATE-bond10" atomRefs="PHENYL-PYRUVATE-atom3 PHENYL-PYRUVATE-atom10" order="2"/> <bond id="PHENYL-PYRUVATE-bond11" atomRefs="PHENYL-PYRUVATE-atom2 PHENYL-PYRUVATE-atom11" order="1"/> <bond id="PHENYL-PYRUVATE-bond12" atomRefs="PHENYL-PYRUVATE-atom1 PHENYL-PYRUVATE-atom8" order="1"/> </bondArray> <formula concise="C 9 H 7 O 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">163.152</float> <string title="smiles">C(=O)([O-])C(CC1(=CC=CC=C1))=O</string> </molecule> </cml> phenylpyruvate phenylpyruvic acid &alpha;-ketohydrocinnamic acid 3-phenyl-2-oxopropanoate keto-phenylpyruvate 2-keto-phenyl-pyruvate MetaCyc PHENYL-PYRUVATE CAS 156-06-9 LIGAND C00166 PubChem 997 1 1 Aromatic amino acid transferase 165.191 L-phenylalanine CML <cml> <molecule id="PHE" title="L-phenylalanine" dictRef="dictPHE"> <atomArray> <atom id="PHE-atom1" elementType="C" x2="1523.0" y2="1136.0"/> <atom id="PHE-atom2" elementType="C" x2="1523.0" y2="1220.0"/> <atom id="PHE-atom3" elementType="C" x2="1596.0" y2="1261.0"/> <atom id="PHE-atom4" elementType="C" x2="1667.0" y2="1220.0"/> <atom id="PHE-atom5" elementType="C" x2="1667.0" y2="1136.0"/> <atom id="PHE-atom6" elementType="C" x2="1596.0" y2="1095.0"/> <atom id="PHE-atom7" elementType="C" x2="1452.0" y2="1095.0"/> <atom id="PHE-atom8" elementType="C" x2="1382.0" y2="1135.0"/> <atom id="PHE-atom9" elementType="C" x2="1310.0" y2="1095.0"/> <atom id="PHE-atom10" elementType="O" x2="1241.0" y2="1135.0" formalCharge="-1"/> <atom id="PHE-atom11" elementType="O" x2="1310.0" y2="1011.0"/> <atom id="PHE-atom12" elementType="N" x2="1382.0" y2="1220.0" formalCharge="1"/> </atomArray> <bondArray> <bond id="PHE-bond1" atomRefs="PHE-atom2 PHE-atom1" order="2"/> <bond id="PHE-bond2" atomRefs="PHE-atom3 PHE-atom2" order="1"/> <bond id="PHE-bond3" atomRefs="PHE-atom4 PHE-atom3" order="2"/> <bond id="PHE-bond4" atomRefs="PHE-atom5 PHE-atom4" order="1"/> <bond id="PHE-bond5" atomRefs="PHE-atom6 PHE-atom5" order="2"/> <bond id="PHE-bond6" atomRefs="PHE-atom1 PHE-atom6" order="1"/> <bond id="PHE-bond7" atomRefs="PHE-atom1 PHE-atom7" order="1"/> <bond id="PHE-bond8" atomRefs="PHE-atom7 PHE-atom8" order="1"/> <bond id="PHE-bond9" atomRefs="PHE-atom8 PHE-atom9" order="1"/> <bond id="PHE-bond10" atomRefs="PHE-atom9 PHE-atom10" order="1"/> <bond id="PHE-bond11" atomRefs="PHE-atom9 PHE-atom11" order="2"/> <bond id="PHE-bond12" atomRefs="PHE-atom8 PHE-atom12" order="1"/> </bondArray> <formula concise="C 9 H 11 N 1 O 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">165.191</float> <string title="smiles">C(=O)([O-])C([N+])CC1(C=CC=CC=1)</string> </molecule> </cml> F endophenyl phenylalanine phe MetaCyc PHE CAS 63-91-2 LIGAND C00079 1 144.084 2-oxoglutarate CML <cml> <molecule id="2-KETOGLUTARATE" title="2-oxoglutarate" dictRef="dict2-KETOGLUTARATE"> <atomArray> <atom id="2-KETOGLUTARATE-atom1" elementType="C" x2="-71940.0" y2="-131190.0"/> <atom id="2-KETOGLUTARATE-atom2" elementType="O" x2="211600.0" y2="-130490.0" formalCharge="-1"/> <atom id="2-KETOGLUTARATE-atom3" elementType="C" x2="141770.0" y2="-89580.0"/> <atom id="2-KETOGLUTARATE-atom4" elementType="O" x2="70530.0" y2="-212300.0"/> <atom id="2-KETOGLUTARATE-atom5" elementType="O" x2="141770.0" y2="-8460.0"/> <atom id="2-KETOGLUTARATE-atom6" elementType="C" x2="70530.0" y2="-131190.0"/> <atom id="2-KETOGLUTARATE-atom7" elementType="O" x2="-212300.0" y2="-130490.0" formalCharge="-1"/> <atom id="2-KETOGLUTARATE-atom8" elementType="C" x2="-700.0" y2="-89580.0"/> <atom id="2-KETOGLUTARATE-atom9" elementType="C" x2="-142480.0" y2="-89580.0"/> <atom id="2-KETOGLUTARATE-atom10" elementType="O" x2="-142480.0" y2="-8460.0"/> </atomArray> <bondArray> <bond id="2-KETOGLUTARATE-bond1" atomRefs="2-KETOGLUTARATE-atom10 2-KETOGLUTARATE-atom9" order="2"/> <bond id="2-KETOGLUTARATE-bond2" atomRefs="2-KETOGLUTARATE-atom9 2-KETOGLUTARATE-atom1" order="1"/> <bond id="2-KETOGLUTARATE-bond3" atomRefs="2-KETOGLUTARATE-atom8 2-KETOGLUTARATE-atom6" order="1"/> <bond id="2-KETOGLUTARATE-bond4" atomRefs="2-KETOGLUTARATE-atom7 2-KETOGLUTARATE-atom9" order="1"/> <bond id="2-KETOGLUTARATE-bond5" atomRefs="2-KETOGLUTARATE-atom6 2-KETOGLUTARATE-atom3" order="1"/> <bond id="2-KETOGLUTARATE-bond6" atomRefs="2-KETOGLUTARATE-atom5 2-KETOGLUTARATE-atom3" order="2"/> <bond id="2-KETOGLUTARATE-bond7" atomRefs="2-KETOGLUTARATE-atom4 2-KETOGLUTARATE-atom6" order="2"/> <bond id="2-KETOGLUTARATE-bond8" atomRefs="2-KETOGLUTARATE-atom2 2-KETOGLUTARATE-atom3" order="1"/> <bond id="2-KETOGLUTARATE-bond9" atomRefs="2-KETOGLUTARATE-atom1 2-KETOGLUTARATE-atom8" order="1"/> </bondArray> <formula concise="C 5 H 4 O 5" formalCharge="0"/> <float title="molecularWeight" units="g/mol">144.084</float> <string title="smiles">C([O-])(=O)C(=O)CCC([O-])=O</string> </molecule> </cml> ketoglutarate &alpha;-ketoglutarate 2-oxoglutaric acid &alpha;-ketoglutaric acid &alpha;-oxoglutarate 2-oxoglutarate 2-ketoglutaric acid 2-ketoglutarate 2-oxopentanedionic acid 2-oxopentanedionate MetaCyc 2-KETOGLUTARATE CAS 328-50-7 LIGAND C00026 ChEBI 30915 LIGAND C00026 PubChem 51 1 Tyrosine transaminase MetaCyc PHEAMINOTRANS-RXN UniProt P04693 RELATED-TO UniProt P74861 RELATED-TO UniProt Q9UWK8 RELATED-TO UniProt Q9UWK9 RELATED-TO UniProt P95468 RELATED-TO UniProt Q9JYA1 RELATED-TO UniProt Q9JT83 RELATED-TO UniProt Q9UZ63 RELATED-TO UniProt O58489 RELATED-TO UniProt O59096 RELATED-TO UniProt Q9PHA8 RELATED-TO UniProt Q9V0L2 RELATED-TO UniProt Q9Z7G5 RELATED-TO UniProt Q02636 RELATED-TO UniProt O84642 RELATED-TO Tyrosine/phenylalanine aminotransferase is one of two enzymes in Bacillus subtilis able to catalyze the terminal reactions in phenylalanine and tyrosine biosynthesis, the other being histidinol-phosphate aminotransferase. Based on kinetic analyses histidinol-phosphate aminotransferase appears to be the primary enzyme involved in tyrosine and phenylalanine synthesis |CITS: [11213] [4431] [BSUB225]|. AROJBACSU-MONOMER AroJ MetaCyc AROJBACSU-MONOMER 1 REVERSIBLE tyrosine/phenylalanine aminotransferase tyrosine transaminase aromatic aminotransferase L-tyrosine:2-oxoglutarate aminotransferase MetaCyc ENZRXN-1561 Phenylalanine transaminase catalyzes the first reaction in the anaerobic oxidation of phenylalanine. |CITS: [9297469]| phenylalanine transaminase Thauera aromatica NCBI Taxonomy 59405 MetaCyc PHETRANTHAUERA-MONOMER 1 REVERSIBLE phenylalanine transaminase MetaCyc ENZRXN-1861 245.128 pyridoxal 5'-phosphate CML <cml> <molecule id="PYRIDOXAL_PHOSPHATE" title="pyridoxal 5'-phosphate" dictRef="dictPYRIDOXAL_PHOSPHATE"> <atomArray> <atom id="PYRIDOXAL_PHOSPHATE-atom1" elementType="C" x2="-5153.0" y2="-2511.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom2" elementType="O" x2="18632.0" y2="-7709.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom3" elementType="O" x2="26735.0" y2="-15813.0" formalCharge="-1"/> <atom id="PYRIDOXAL_PHOSPHATE-atom4" elementType="P" x2="18632.0" y2="-15813.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom5" elementType="C" x2="-19512.0" y2="-2511.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom6" elementType="N" x2="-12288.0" y2="1631.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom7" elementType="C" x2="-12288.0" y2="-14930.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom8" elementType="C" x2="1805.0" y2="-15813.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom9" elementType="O" x2="-4978.0" y2="-26824.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom10" elementType="O" x2="10791.0" y2="-15813.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom11" elementType="C" x2="-19512.0" y2="-10880.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom12" elementType="O" x2="18632.0" y2="-23916.0" formalCharge="-1"/> <atom id="PYRIDOXAL_PHOSPHATE-atom13" elementType="C" x2="-12288.0" y2="-23125.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom14" elementType="C" x2="-5153.0" y2="-10880.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom15" elementType="C" x2="-26824.0" y2="925.0"/> <atom id="PYRIDOXAL_PHOSPHATE-atom16" elementType="O" x2="-26118.0" y2="-15547.0"/> </atomArray> <bondArray> <bond id="PYRIDOXAL_PHOSPHATE-bond1" atomRefs="PYRIDOXAL_PHOSPHATE-atom16 PYRIDOXAL_PHOSPHATE-atom11" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond2" atomRefs="PYRIDOXAL_PHOSPHATE-atom15 PYRIDOXAL_PHOSPHATE-atom5" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond3" atomRefs="PYRIDOXAL_PHOSPHATE-atom14 PYRIDOXAL_PHOSPHATE-atom8" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond4" atomRefs="PYRIDOXAL_PHOSPHATE-atom13 PYRIDOXAL_PHOSPHATE-atom7" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond5" atomRefs="PYRIDOXAL_PHOSPHATE-atom12 PYRIDOXAL_PHOSPHATE-atom4" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond6" atomRefs="PYRIDOXAL_PHOSPHATE-atom11 PYRIDOXAL_PHOSPHATE-atom5" order="2"/> <bond id="PYRIDOXAL_PHOSPHATE-bond7" atomRefs="PYRIDOXAL_PHOSPHATE-atom7 PYRIDOXAL_PHOSPHATE-atom11" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond8" atomRefs="PYRIDOXAL_PHOSPHATE-atom10 PYRIDOXAL_PHOSPHATE-atom4" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond9" atomRefs="PYRIDOXAL_PHOSPHATE-atom9 PYRIDOXAL_PHOSPHATE-atom13" order="2"/> <bond id="PYRIDOXAL_PHOSPHATE-bond10" atomRefs="PYRIDOXAL_PHOSPHATE-atom8 PYRIDOXAL_PHOSPHATE-atom10" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond11" atomRefs="PYRIDOXAL_PHOSPHATE-atom14 PYRIDOXAL_PHOSPHATE-atom7" order="2"/> <bond id="PYRIDOXAL_PHOSPHATE-bond12" atomRefs="PYRIDOXAL_PHOSPHATE-atom6 PYRIDOXAL_PHOSPHATE-atom1" order="2"/> <bond id="PYRIDOXAL_PHOSPHATE-bond13" atomRefs="PYRIDOXAL_PHOSPHATE-atom5 PYRIDOXAL_PHOSPHATE-atom6" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond14" atomRefs="PYRIDOXAL_PHOSPHATE-atom3 PYRIDOXAL_PHOSPHATE-atom4" order="1"/> <bond id="PYRIDOXAL_PHOSPHATE-bond15" atomRefs="PYRIDOXAL_PHOSPHATE-atom2 PYRIDOXAL_PHOSPHATE-atom4" order="2"/> <bond id="PYRIDOXAL_PHOSPHATE-bond16" atomRefs="PYRIDOXAL_PHOSPHATE-atom1 PYRIDOXAL_PHOSPHATE-atom14" order="1"/> </bondArray> <formula concise="C 8 H 8 N 1 O 6 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">245.128</float> <string title="smiles">C1(C(=C(C(=C(N=1)C)O)C=O)COP(=O)([O-])[O-])</string> </molecule> </cml> PLP pyridoxal phosphate pyridoxal-5P pyridoxal 5-phosphate pyridoxal-P MetaCyc PYRIDOXAL_PHOSPHATE CAS 54-47-7 LIGAND C00018 1 Histidinol-phosphate aminotransferase is primarily an enzyme in histidine biosynthesis. However the enzyme can catalyze the terminal reactions in the biosynthesis of tyrosine and phenylalanine. Histidinol-phosphate aminotransferase is one of two enzymes in Bacillus subtilis able to catalyze these terminal reactions, the other is aromatic aminotransferase. Based on kinetic analyses histidinol-phosphate aminotransferase appears to be the primary enzyme involved in tyrosine and phenylalanine synthesis |CITS: [11213] [4431] [BSUB225]|. HISCBACSU-MONOMER HisH HisC MetaCyc HISCBACSU-MONOMER 1 histidinol-phosphate aminotransferase imidazole acetol-phosphate transaminase imidazolylacetolphosphate transaminase MetaCyc ENZRXN-12331 |FRAME: TAX-559292| possesses at least two aromatic aminotransferase (labeled I and II), encoded by |FRAME:G-9201| and |FRAME:G-9202|, respectively. The roles of |FRAME:MONOMER-11841| are not completely clear. It is a constitutive enzyme clearly involved in the biosynthesis of |FRAME:TRP|, |FRAME:PHE|, and |FRAME:TYR|, with a 20-fold higher affinity for |FRAME:TYR| and |FRAME:PHE| than for |FRAME:TRP| |CITS:[6763508]|. However, <i>aro8</i> mutants fail to grow when the nitrogen source is either of these three amino acids, although the data suggests that this failure is not attributable in all cases to a blocked first transamination step |CITS: [9491082]|. Thus, the exact role played by |FRAME:MONOMER-11841| in the catabolism of the aromatic amino acids is still not completely clear. |FRAME:MONOMER-11842|, on the other hand, is an inducible enzyme, and is clearly catabolic. Its main responsibility is likely the degradation of |FRAME:TRP| (see |FRAME:PWY-5081|) |CITS: [9491082]|. aromatic amino acid aminotransferase I Saccharomyces cerevisiae subsp. S288c NCBI Taxonomy 559292 MetaCyc MONOMER-11841 UniProt P53090 Swiss-Model P53090 ModBase P53090 1 aromatic amino acid aminotransferase MetaCyc ENZRXN-12332 1 The Kcat for phenylalanine is 824/minute |CITS: [11736651]|. Aspartate aminotransferase (AspC) is a multifunctional enzyme that catalyzes the synthesis of aspartate, phenylalanine and other compounds via a transamination reaction. AspC catalyzes the synthesis of aspartate, phenylalanine, and kynurenate |CITS:[3521591][15983][323238][352693][2082822][10356262][11736651]|. This reaction is catalyzed via a ping-pong Bi-Bi mechanism in which the cofactor alternates between the pyridoxal phosphate and pyridoxamine forms |CITS:[1993208]|. An amino acid substrate binds via an aldimine bond to pyridoxal phosphate, after which a hydrogen atom is removed from the substrate. This deprotonation yields a quinonoid intermediate, which is followed by addition of a proton to the coenzyme and the formation of a ketimine intermediate. This intermediate is then hydrolyzed to form a keto acid substrate and the pyridoxamine form of the enzyme. This reaction mechanism has been studied extensively |CITS: [3907632][2201406][1907854][7696265][7588727][8611515][9790670][11148029][12488449][12966078]|. AspC is catalytically active as a dimer |CITS: [1572361]|. A crystal structure of AspC to 2.5 &Aring; resolution showed that each of its subunits has a large and a small domain as well as one bound pyridoxal 5'-phosphate |CITS: [2121725]|. Many crystal structures have been generated for AspC and mutant variants of AspC, in both bound and unbound states, usually to resolutions in the 2-3 &Aring; range |CITS: [3543379][2513875][1993208][8436109][7909946][8073030][8196059][7819232][9893985]|. Crystal structures of AspC bound to inhibitors reveal that they operate by closing up the active site |CITS: [7798192]|. In the case of maleate, this occurs after maleate itself occupies the active site |CITS: [7896726]|. Structures of several cysteine mutants show that alteration of non-active-site residues can also affect the conformation of the active site |CITS: [10708649]|. The active site has also been studied via NMR |CITS: [9012676]|. A number of studies have looked at the residues around and in the active site, as well as their interaction with pyridoxal 5'-phosphate (note that some of the residue numbers given in these studies do not precisely match the locations of those residues in the current sequence for AspC, but they do refer to this protein) |CITS: [1993208][2007566][1677269][1868057][1610831][8263922][8439541][8347609][8177890][8188615]|. AspC can be mutated to alter its activity to that of a tyrosine transaminase of roughly equivalent efficacy |CITS: [7664122][8528073][12634055][14767072][15461450]|. It has been mutated to develop other changes in substrate specificity as well |CITS: [7556224][9268327][10531314]|. The specificity of AspC has even been altered by mutations in residues that are not a part of the active site |CITS: [9891001]|. AspC B0928 AspC MetaCyc ASPAMINOTRANS-MONOMER UniProt P00509 PDB 1AAM PDB 1AAW PDB 1AIA PDB 1AIB PDB 1AIC PDB 1AMQ PDB 1AMR PDB 1AMS PDB 1ARS PDB 1ART PDB 1ASA PDB 1ASB PDB 1ASC PDB 1ASD PDB 1ASE PDB 1ASF PDB 1ASG PDB 1ASL PDB 1ASM PDB 1ASN PDB 1SPA PDB 2AAT PDB 3AAT PDB 1AHE PDB 1AHF PDB 1AHG PDB 1AHX PDB 1AHY PDB 1ARG PDB 1ARH PDB 1ARI PDB 1B4X PDB 1BQA PDB 1BQD PDB 1G4V PDB 1G4X PDB 1G7W PDB 1G7X PDB 1IX6 PDB 1IX7 PDB 1IX8 PDB 1QIR PDB 1QIS PDB 1QIT PDB 1YOO PDB 5EAA RefSeq NP_415448 PDB 1CQ8 Pfam PF00155 IN-FAMILY ModBase P00509 EcoliWiki b0928 2 aspartate aminotransferase, PLP-dependent MetaCyc ASPAMINOTRANS-DIMER Gelfand DH Rudo N PubMed 323238 J Bacteriol 130(1);441-4 Mapping of the aspartate and aromatic amino acid aminotransferase genes tyrB and aspC. 1977 Kondo K Wakabayashi S Kagamiyama H PubMed 3298240 J Biol Chem 1987;262(18);8648-57 Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure. 1987 Fotheringham IG Dacey SA Taylor PP Smith TJ Hunter MG Finlay ME Primrose SB Parker DM Edwards RM PubMed 3521591 Biochem J 1986;234(3);593-604 The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. 1986 Kuramitsu S Okuno S Ogawa T Ogawa H Kagamiyama H PubMed 3897210 J Biochem (Tokyo) 97(4);1259-62 Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene. 1985 Kondo K Wakabayashi S Yagi T Kagamiyama H PubMed 6378205 Biochem Biophys Res Commun 122(1);62-7 The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes. 1984 1 aromatic-amino-acid transaminase aromatic-amino-acid:2-oxoglutarate aminotransferase aromatic aminotransferase MetaCyc ENZRXN0-6321 1 dditional kinetic data pertaining to phenylalanine, phenylpyruvate, and oxaloacetate have been determined |CITS: [236311][15983]|. Tyrosine aminotransferase (TyrB), also known as aromatic-acid aminotransferase, is a broad-specificity enzyme that catalyzes the final step in tyrosine, leucine, and phenylalanine biosynthesis. TyrB catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively |CITS: [4404056][15983][236311][361681]|. It overlaps with the catalytic activities of |FRAME: BRANCHED-CHAINAMINOTRANSFER-CPLX| (IlvE), which also produces leucine, and |FRAME: ASPAMINOTRANS-DIMER| (AspC), which also produces phenylalanine. In the latter case, however, TyrB is 1,000-fold more active toward aromatic substrates than AspC |CITS: [8218300]|. TyrB is repressible by two of its products, leucine and tyrosine, and a precursor in the leucine biosynthesis pathway, keto-isovalerate |CITS: [4404056][361681][1646790]|. The last case has been shown to occur by direct inhibition of TyrB enzymatic function |CITS: [1646790]|. The mechanism of action of TyrB has been examined, especially around the PLP-binding site |CITS: [11112527][8188625]|. The nature of TyrB substrate specificity has also been studied |CITS: [8528072][8639626]|. TyrB exists as a dimer |CITS: [352693]|. A crystal structure of TyrB with bound PLP has been determined to 3.5 &Aring; resolution |CITS: [10417420]|. TyrB B4054 TyrB MetaCyc TYRB-MONOMER UniProt P04693 PDB 3TAT RefSeq NP_418478 Pfam PF00155 IN-FAMILY ModBase P04693 EcoliWiki b4054 Kuramitsu S Inoue K Ogawa T Ogawa H Kagamiyama H PubMed 3907634 Biochem Biophys Res Commun 1985;133(1);134-9 Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene. 1985 2 tyrosine aminotransferase tyrosine aminotransferase, tyrosine-repressible, PLP-dependent aromatic-amino-acid transaminase MetaCyc TYRB-DIMER 1 REVERSIBLE phenylalanine aminotransferase aromatic-amino-acid: 2-oxoglutarate aminotransferase MetaCyc PHEAMINOTRANS-ENZRXN Prephenate is the last common precursor of phenylalanine and tyrosine. Prephenate dehydratase converts prephenate to phenylpyruvate. Prephenate dehydratase can exist in different states: an inactive monomer, a fully active octamer and a variably active dimer. Association and dissociation occurs under the influence of the allosteric effectors phenylalanine, methionine, leucine and tryptophan. |CITS: [114523] [3110557] [104661] [4992710] [BSUB225] [4964627] [4956345]| 4.2.1.51 1 224.17 prephenate CML <cml> <molecule id="PREPHENATE" title="prephenate" dictRef="dictPREPHENATE"> <atomArray> <atom id="PREPHENATE-atom1" elementType="C" x2="-15388.0" y2="2935.0"/> <atom id="PREPHENATE-atom2" elementType="C" x2="-15388.0" y2="-11342.0"/> <atom id="PREPHENATE-atom3" elementType="C" x2="-19592.0" y2="-4125.0"/> <atom id="PREPHENATE-atom4" elementType="C" x2="-3013.0" y2="-4125.0"/> <atom id="PREPHENATE-atom5" elementType="C" x2="15071.0" y2="-15150.0"/> <atom id="PREPHENATE-atom6" elementType="C" x2="-7138.0" y2="2935.0"/> <atom id="PREPHENATE-atom7" elementType="C" x2="3252.0" y2="1825.0"/> <atom id="PREPHENATE-atom8" elementType="O" x2="3252.0" y2="9837.0"/> <atom id="PREPHENATE-atom9" elementType="O" x2="11263.0" y2="1825.0" formalCharge="-1"/> <atom id="PREPHENATE-atom10" elementType="C" x2="3252.0" y2="-9677.0"/> <atom id="PREPHENATE-atom11" elementType="C" x2="11581.0" y2="-9677.0"/> <atom id="PREPHENATE-atom12" elementType="O" x2="17292.0" y2="-4046.0"/> <atom id="PREPHENATE-atom13" elementType="O" x2="15071.0" y2="-23161.0"/> <atom id="PREPHENATE-atom14" elementType="C" x2="-7138.0" y2="-11342.0"/> <atom id="PREPHENATE-atom15" elementType="O" x2="-22527.0" y2="-7933.0"/> <atom id="PREPHENATE-atom16" elementType="O" x2="23082.0" y2="-15150.0" formalCharge="-1"/> </atomArray> <bondArray> <bond id="PREPHENATE-bond1" atomRefs="PREPHENATE-atom16 PREPHENATE-atom5" order="1"/> <bond id="PREPHENATE-bond2" atomRefs="PREPHENATE-atom15 PREPHENATE-atom3" order="1"/> <bond id="PREPHENATE-bond3" atomRefs="PREPHENATE-atom14 PREPHENATE-atom4" order="1"/> <bond id="PREPHENATE-bond4" atomRefs="PREPHENATE-atom13 PREPHENATE-atom5" order="2"/> <bond id="PREPHENATE-bond5" atomRefs="PREPHENATE-atom12 PREPHENATE-atom11" order="2"/> <bond id="PREPHENATE-bond6" atomRefs="PREPHENATE-atom11 PREPHENATE-atom10" order="1"/> <bond id="PREPHENATE-bond7" atomRefs="PREPHENATE-atom10 PREPHENATE-atom4" order="1"/> <bond id="PREPHENATE-bond8" atomRefs="PREPHENATE-atom9 PREPHENATE-atom7" order="1"/> <bond id="PREPHENATE-bond9" atomRefs="PREPHENATE-atom8 PREPHENATE-atom7" order="2"/> <bond id="PREPHENATE-bond10" atomRefs="PREPHENATE-atom7 PREPHENATE-atom4" order="1"/> <bond id="PREPHENATE-bond11" atomRefs="PREPHENATE-atom6 PREPHENATE-atom4" order="1"/> <bond id="PREPHENATE-bond12" atomRefs="PREPHENATE-atom5 PREPHENATE-atom11" order="1"/> <bond id="PREPHENATE-bond13" atomRefs="PREPHENATE-atom3 PREPHENATE-atom2" order="1"/> <bond id="PREPHENATE-bond14" atomRefs="PREPHENATE-atom2 PREPHENATE-atom14" order="2"/> <bond id="PREPHENATE-bond15" atomRefs="PREPHENATE-atom1 PREPHENATE-atom3" order="1"/> <bond id="PREPHENATE-bond16" atomRefs="PREPHENATE-atom1 PREPHENATE-atom6" order="2"/> </bondArray> <formula concise="C 10 H 8 O 6" formalCharge="0"/> <float title="molecularWeight" units="g/mol">224.17</float> <string title="smiles">C(C(CC1(C=CC(C=C1)O)(C(=O)[O-]))=O)(=O)[O-]</string> <string title="systematicName">Prephenic acid</string> </molecule> </cml> MetaCyc PREPHENATE CAS 126-49-8 LIGAND C00254 1 Prephenate dehydratase 1 1 1 MetaCyc PREPHENATEDEHYDRAT-RXN UniProt P32452 UniProt P43909 UniProt Q02286 RELATED-TO UniProt P0A9J8 RELATED-TO UniProt Q9PII3 RELATED-TO UniProt Q9CEU2 UniProt Q58054 UniProt P21203 UniProt P43900 RELATED-TO UniProt P27603 RELATED-TO Prephenate dehydratase can exist in different states: an inactive monomer, a fully active octamer and a variably active dimer. Association and dissociation occurs under the influence of allosteric effectors. |CITS: [114523] [3110557]| PheA PheA MetaCyc PHEABACSU-MONOMER 8 CPLX-1161 MetaCyc CPLX-1161 1 REVERSIBLE prephenate dehydratase PDT prephenate hydro-lyase (decarboxylating) MetaCyc ENZRXN-1521 This is the second of two reactions catalyzed by one dimeric protein. There are two closely similar two-reaction enzymes in E. coli, encoded by the pheA and tyrA genes. This is the pheA enzyme reaction. There are two cysteine residues at or close to the prephenate dehydratase active site and both may be essential for the prephenate dehydratase activity |CITS:[3881132]| The N-terminal end of this bifunctional protein specifies the chorismate mutase activity while the remainder of the sequence specifies the second enzymatic activity, prephenate dehydratase. The native enzyme is a dimer of identical subunits each containing a dehydratase active site, a mutase active site and a phenylalanine binding site.|CITS:[334530]| The chorismate mutase and prephenate dehydratase reactions occur at separate active sites. In contrast, the two active sites of the closely related enzyme chorismate mutase/prephenate dehydrogenase are interacting sites. |CITS: [6395895]| Studies of the overall reaction using radioactive chorismate showed that prephenate, which is formed from chorismate, dissociates from the mutase site and equilibrates with the bulk medium before combining at the dehydratase site. Also,the two activities are subject to differential inhibition. |CITS:[348236]| Further, the mutase site contains a lysine residue which is not essential for dehydratase activity and the dehydratase site contains a cysteine and a threonine residue neither of which is required for mutase activity. |CITS:[6337635]| Differential inactivation of the dehydratase and mutase activities by modification of the most reactive sulfhydryl group provides evidence that the two activities are catalyzed at separate sites on the enzyme, or at sites that only overlap slightly. |CITS:[334529]| PheA B2599 PheA MetaCyc CHORISMUTPREPHENDEHYDRAT-MONOMER PDB 1ECM RefSeq NP_417090 UniProt P0A9J8 Pfam PF01817 IN-FAMILY Swiss-Model P0A9J8 ModBase P0A9J8 EcoliWiki b2599 2 CHORISMUTPREPHENDEHYDRAT-CPLX MetaCyc CHORISMUTPREPHENDEHYDRAT-CPLX Bose KS Sarma RH PubMed 2 Biochem Biophys Res Commun 1975;66(4);1173-9 Delineation of the intimate details of the backbone conformation of pyridine nucleotide coenzymes in aqueous solution. 1975 Makar AB McMartin KE Palese M Tephly TR PubMed 1 Biochem Med 1975;13(2);117-26 Formate assay in body fluids: application in methanol poisoning. 1975 1 IRREVERSIBLE-LEFT-TO-RIGHT prephenate dehydratase chorismate mutase prephenate dehydratase chorismate mutase-prephenate hydrolyase(decarboxylating) MetaCyc PREPHENATEDEHYDRAT-ENZRXN Ma KH Davidson BE PubMed 3881132 Biochim Biophys Acta 1985;827(1);1-7 The reactivity of the sulphydryl groups of chorismate mutase/prephenate dehydratase--a bifunctional enzyme of phenylalanine biosynthesis in Escherichia coli K12. 1985 Baldwin GS Davidson BE PubMed 6337635 Biochim Biophys Acta 1983;742(2);374-83 Kinetic studies on the mechanism of chorismate mutase/prephenate dehydratase from Escherichia coli K12. 1983 The aroA encoded protein is a bifunctional enzyme consisting of DAHP synthase and chorismate mutase. Both are enzymes of aromatic amino acid synthesis. There is evidence that DAHP synthase-chorismate mutase also activates another enzyme of the same pathway, shikimate kinase. Chorismate mutase is located at the branch point of the shikimate pathway, from which the aromatic amino acids are synthesized. Chorismate mutase channels amino acid precursors to phenylalanine and tyrosine biosynthesis and away from tryptophan biosynthesis. In some strains of Bacillus subtilis there are two chorismate mutase activities. One is the aroA-encoded DAHP synthase-chorismate mutase and the other is a monofunctional enzyme encoded by aroH. Neither enzyme is regulated by end-product amino acids, but both are inhibited by prephenate. |CITS: [4210506] [4211044] [6101597] [4962501] [JMB12-468] [BSUB225] [4626882] [BSUB225] [8046752] [2105742] [4996881] [9457377]| 5.4.99.5 1 Chorismate mutase 1 MetaCyc CHORISMATEMUT-RXN UniProt O22410 UniProt O22409 UniProt P42738 UniProt Q02287 RELATED-TO UniProt Q02286 RELATED-TO UniProt P07023 RELATED-TO UniProt P0A9J8 RELATED-TO UniProt Q9PII3 RELATED-TO UniProt P43902 RELATED-TO UniProt Q57696 UniProt Q58029 UniProt P21204 UniProt Q9RQV7 UniProt P43900 RELATED-TO UniProt P32178 UniProt P27603 RELATED-TO UniProt P19080 1 REVERSIBLE chorismate mutase hydroxyphenylpyruvate synthase chorismate pyruvatemutase MetaCyc ENZRXN-1421 Chorismate mutase is located at the branch point of the shikimate pathway, from which the aromatic amino acids are synthesized. Chorismate mutase channels amino acid precursors to phenylalanine and tyrosine biosynthesis and away from tryptophan biosynthesis. In some strains of Bacillus subtilis there are two chorismate mutase activities. One is the aroA-encoded DAHP synthase-chorismate mutase and the other is a monofunctional enzyme encoded by aroH. Neither enzyme is regulated by end-product amino acids, but both are inhibited by prephenate. |CITS: [BSUB225] [8046752] [2105742] [4996881] [9457377]| AroH AroH MetaCyc AROHBACSU-MONOMER 3 CPLX-1141 MetaCyc CPLX-1141 1 REVERSIBLE chorismate mutase chorismate mutase, monofunctional CM hydroxyphenylpyruvate synthase chorismate pyruvatemutase MetaCyc ENZRXN-1501 Three genes encoding chorismate mutase exist in Arabidopsis. AtCM1 and CM-3 are the plastidic isoforms, and AtCM2 the cytosolic isoform. The three genes are expressed in different tissues. In addition, AtCM1 is elicitor- and pathogen induced. Enzymatic activities of the three isoforms were demonstrated by complementing an E.coli and a yeast chorismate mutase-deficient strain. The enzymatic activities of AtCM1 and CM-3 are inhibited by phenylalanine and tyrosine, whereas the enzymatic activity of AtCM2 is not affected. Whilst the role of AtCM1 and CM-3 in tyrosine and phenylalanine biosynthesis is sound, the physiological role of AtCM2 is not clear. AT3G29200-MONOMER Arabidopsis thaliana col MetaCyc AT3G29200-MONOMER Mobley EM Kunkel BN Keith B PubMed 10564818 Gene 240(1);115-23 Identification, characterization and comparative analysis of a novel chorismate mutase gene in Arabidopsis thaliana. 1999 Eberhard J Ehrler TT Epple P Felix G Raesecke HR Amrhein N Schmid J PubMed 8953244 Plant J 10(5);815-21 Cytosolic and plastidic chorismate mutase isozymes from Arabidopsis thaliana: molecular characterization and enzymatic properties. 1996 CCO-CHLOROPLAST GO GO:0009507 1 chorismate mutase MetaCyc ENZRXN-8221 Three genes encoding chorismate mutase exist in Arabidopsis. AtCM1 and CM-3 are the plastidic isoforms, and AtCM2 the cytosolic isoform. The three genes are expressed in different tissues. In addition, AtCM1 is elicitor- and pathogen induced. Enzymatic activities of the three isoforms were demonstrated by complementing an E.coli and a yeast chorismate mutase-deficient strain. The enzymatic activities of AtCM1 and CM-3 are inhibited by phenylalanine and tyrosine, whereas the enzymatic activity of AtCM2 is not affected. Whilst the role of AtCM1 and CM-3 in tyrosine and phenylalanine biosynthesis is sound, the physiological role of AtCM2 is not clear. AT5G10870-MONOMER MetaCyc AT5G10870-MONOMER 1 chorismate mutase MetaCyc ENZRXN-8222 Three genes encoding chorismate mutase exist in Arabidopsis. AtCM1 and CM-3 are the plastidic isoforms, and AtCM2 the cytosolic isoform. The three genes are expressed in different tissues. In addition, AtCM1 is elicitor- and pathogen induced. Enzymatic activities of the three isoforms were demonstrated by complementing an E.coli and a yeast chorismate mutase-deficient strain. The enzymatic activities of AtCM1 and CM-3 are inhibited by phenylalanine and tyrosine, whereas the enzymatic activity of AtCM2 is not affected. Whilst the role of AtCM1 and CM-3 in tyrosine and phenylalanine biosynthesis is sound, the physiological role of AtCM2 is not clea AT1G69370-MONOMER MetaCyc AT1G69370-MONOMER 1 chorismate mutase MetaCyc ENZRXN-8223 An alternate Km value of 140 &micro;M has been reported for chorismate |CITS: [6809460]|. The Km for chorismate has been reported to shift to 40 &micro;M in the presence of NAD+ |CITS: [6338013]|. Tyrosine cooperatively inhibits chorismate mutase activity in the presence of NAD+, although it never surpasses 50% inhibition of the reaction. NAD+ and tyrosine both dramatically increase the affinity of the enzyme for each other |CITS: [6338013]|. Contrasting research has shown that tyrosine is only a marginal inhibitor of chorismate mutase activity |CITS: [16269762]|. Bifunctional chorismate mutase / prephenate dehydrogenase (TyrA) carries out the shared first step in the parallel biosynthetic pathways for the aromatic amino acids tyrosine and phenylalanine, as well as the second step in tyrosine biosynthesis. TyrA catalyzes both the conversion of chorismate into prephenate and the subsequent NAD+-dependent oxidative decarboxylation of prephenate |CITS: [5326114][7044424][4929151][4929152]|. The two catalytic activities of TyrA occur in separate portions of the protein, and are partially separable via mutation. Specifically, the chorismate mutase activity requires the amino-terminal portion of the protein, and the prephenate dehydrogenase activity is in the carboxy-terminal portion of the protein. Each isolated activity is markedly diminished when compared with its normal levels in whole TyrA |CITS: [12581215]|. The dehydrogenase activity can also be deactivated via point mutations that disrupt NAD+ binding. These mutations do not, in turn, disable chorismate mutase function |CITS: [6809460][3308859]|. A single sulfhydryl group within the protein is critical for both activities, despite their apparent localizations in different portions of the protein |CITS: [6395895]|. TyrA can occur as both a dimer and a tetramer. It is typically detected as an active dimer, and even the isolated amino- and carboy-terminal portions described above can dimerize independent of their missing halves |CITS: [6809460][6395895][12581215]|. A mol of dimerized TyrA can bind roughly one mol of NAD+, one mol of tyrosine, or one mol of prephenate. In the simultaneous presence of NAD+ and tyrosine, TyrA forms a tetramer rather than a dimer |CITS: [6338013]|. In addition to the 88 kD value, molecular weights of 78.8 kD for the dimer and 136 kD for the tetrameric form have been reported |CITS: [6338013][6338013]|. TyrA B2600 TyrA MetaCyc CHORISMUTPREPHENDEHYDROG-MONOMER UniProt P07023 RefSeq NP_417091 Pfam PF01817 IN-FAMILY ModBase P07023 EcoliWiki b2600 2 CHORISMUTPREPHENDEHYDROG-CPLX MetaCyc CHORISMUTPREPHENDEHYDROG-CPLX 1 chorismate mutase chorismate mutase-prephenate:NAD+ oxidoreductase(decarboxylating) chorismate mutase prephenate dehydrogenase MetaCyc CHORISMATEMUT1-ENZRXN This reaction is the first step after chorismate in the biosynthesis of both phenylalanine and tyrosine. The chorismate mutase reaction is one of two reactions catalyzed by a single dimeric protein. There are two closely similar two-reaction enzymes in E. coli, encoded by the pheA and tyrA genes. For phenylalanine synthesis, in the relevant reaction chorismate is rearranged to form prephenate which subsequently undergoes oxidative decarboxylation to yield phenylpyruvate, the keto equivalent of phenylalanine. The role of chorismate mutase in catalyzing the rearrangement may be to invert the conformation of the chorismate ring so as to orientate the side chain correctly for rearrangement to occur.|CITS:[6337635]| 1 REVERSIBLE chorismate mutase chorismate mutase-prephenate hydrolyase(decarboxylating) chorismate mutase prephenate dehydratase MetaCyc CHORISMATEMUT2-ENZRXN Baldwin GS Davidson BE PubMed 7030214 Arch Biochem Biophys 1981;211(1);66-75 A kinetic and structural comparison of chorismate mutase/prephenate dehydratase from mutant strains of Escherichia coli K 12 defective in the PheA gene. 1981 2.6.1.57 179.152 4-hydroxyphenylpyruvate CML <cml> <molecule id="P-HYDROXY-PHENYLPYRUVATE" title="4-hydroxyphenylpyruvate" dictRef="dictP-HYDROXY-PHENYLPYRUVATE"> <atomArray> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom1" elementType="O" x2="5000.0" y2="-1238.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom2" elementType="O" x2="3571.0" y2="-412.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom3" elementType="O" x2="4286.0" y2="-2474.0" formalCharge="-1"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom4" elementType="O" x2="0.0" y2="0.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom5" elementType="C" x2="714.0" y2="-1238.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom6" elementType="C" x2="1429.0" y2="0.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom7" elementType="C" x2="1429.0" y2="-1650.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom8" elementType="C" x2="2142.0" y2="-412.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom9" elementType="C" x2="2857.0" y2="-1650.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom10" elementType="C" x2="4286.0" y2="-1650.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom11" elementType="C" x2="3571.0" y2="-1238.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom12" elementType="C" x2="714.0" y2="-412.0"/> <atom id="P-HYDROXY-PHENYLPYRUVATE-atom13" elementType="C" x2="2142.0" y2="-1238.0"/> </atomArray> <bondArray> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond1" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom1 P-HYDROXY-PHENYLPYRUVATE-atom10" order="2"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond2" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom2 P-HYDROXY-PHENYLPYRUVATE-atom11" order="2"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond3" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom3 P-HYDROXY-PHENYLPYRUVATE-atom10" order="1"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond4" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom4 P-HYDROXY-PHENYLPYRUVATE-atom12" order="1"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond5" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom5 P-HYDROXY-PHENYLPYRUVATE-atom7" order="2"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond6" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom12 P-HYDROXY-PHENYLPYRUVATE-atom5" order="1"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond7" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom8 P-HYDROXY-PHENYLPYRUVATE-atom6" order="1"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond8" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom6 P-HYDROXY-PHENYLPYRUVATE-atom12" order="2"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond9" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom7 P-HYDROXY-PHENYLPYRUVATE-atom13" order="1"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond10" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom13 P-HYDROXY-PHENYLPYRUVATE-atom8" order="2"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond11" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom9 P-HYDROXY-PHENYLPYRUVATE-atom11" order="1"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond12" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom9 P-HYDROXY-PHENYLPYRUVATE-atom13" order="1"/> <bond id="P-HYDROXY-PHENYLPYRUVATE-bond13" atomRefs="P-HYDROXY-PHENYLPYRUVATE-atom10 P-HYDROXY-PHENYLPYRUVATE-atom11" order="1"/> </bondArray> <formula concise="C 9 H 7 O 4" formalCharge="0"/> <float title="molecularWeight" units="g/mol">179.152</float> <string title="smiles">C(C(CC1(=CC=C(C=C1)O))=O)([O-])=O</string> </molecule> </cml> p-hydroxyphenylpyruvic acid 3-(4-hydroxyphenyl)pyruvate hydroxyphenylpyruvate <i>p</i>-hydroxyphenylpyruvate MetaCyc P-HYDROXY-PHENYLPYRUVATE LIGAND C01179 PubChem 979 CAS 156-39-8 1 1 Aromatic amino acid transferase 181.191 L-tyrosine CML <cml> <molecule id="TYR" title="L-tyrosine" dictRef="dictTYR"> <atomArray> <atom id="TYR-atom1" elementType="C" x2="-10302.0" y2="-1530.0"/> <atom id="TYR-atom2" elementType="C" x2="-18090.0" y2="-4318.0"/> <atom id="TYR-atom3" elementType="C" x2="-4046.0" y2="-6936.0"/> <atom id="TYR-atom4" elementType="N" x2="-10302.0" y2="6597.0" formalCharge="1"/> <atom id="TYR-atom5" elementType="O" x2="-24755.0" y2="442.0" formalCharge="-1"/> <atom id="TYR-atom6" elementType="O" x2="-18259.0" y2="-11765.0"/> <atom id="TYR-atom7" elementType="C" x2="3060.0" y2="-2789.0"/> <atom id="TYR-atom8" elementType="C" x2="3060.0" y2="5440.0"/> <atom id="TYR-atom9" elementType="C" x2="10201.0" y2="-6936.0"/> <atom id="TYR-atom10" elementType="C" x2="10201.0" y2="9555.0"/> <atom id="TYR-atom11" elementType="C" x2="17376.0" y2="-2789.0"/> <atom id="TYR-atom12" elementType="C" x2="17376.0" y2="5440.0"/> <atom id="TYR-atom13" elementType="O" x2="24450.0" y2="9521.0"/> </atomArray> <bondArray> <bond id="TYR-bond1" atomRefs="TYR-atom11 TYR-atom12" order="2"/> <bond id="TYR-bond2" atomRefs="TYR-atom12 TYR-atom13" order="1"/> <bond id="TYR-bond3" atomRefs="TYR-atom12 TYR-atom10" order="1"/> <bond id="TYR-bond4" atomRefs="TYR-atom9 TYR-atom11" order="1"/> <bond id="TYR-bond5" atomRefs="TYR-atom10 TYR-atom8" order="2"/> <bond id="TYR-bond6" atomRefs="TYR-atom7 TYR-atom9" order="2"/> <bond id="TYR-bond7" atomRefs="TYR-atom8 TYR-atom7" order="1"/> <bond id="TYR-bond8" atomRefs="TYR-atom3 TYR-atom7" order="1"/> <bond id="TYR-bond9" atomRefs="TYR-atom2 TYR-atom6" order="2"/> <bond id="TYR-bond10" atomRefs="TYR-atom2 TYR-atom5" order="1"/> <bond id="TYR-bond11" atomRefs="TYR-atom4 TYR-atom1" order="1"/> <bond id="TYR-bond12" atomRefs="TYR-atom1 TYR-atom3" order="1"/> <bond id="TYR-bond13" atomRefs="TYR-atom1 TYR-atom2" order="1"/> </bondArray> <formula concise="C 9 H 11 N 1 O 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">181.191</float> <string title="smiles">C(C(CC1(C=CC(O)=CC=1))[N+])([O-])=O</string> </molecule> </cml> Y tyr tyrosine MetaCyc TYR CAS 60-18-4 LIGAND C00082 1 1 MetaCyc TYRAMINOTRANS-RXN UniProt P04693 RELATED-TO UniProt P74861 RELATED-TO UniProt Q9UWK8 RELATED-TO UniProt Q9UWK9 RELATED-TO UniProt P95468 RELATED-TO UniProt Q9JYA1 RELATED-TO UniProt Q9JT83 RELATED-TO UniProt Q9UZ63 RELATED-TO UniProt O58489 RELATED-TO UniProt O59096 RELATED-TO UniProt Q9PHA8 RELATED-TO UniProt Q9V0L2 RELATED-TO UniProt Q9Z7G5 RELATED-TO UniProt Q02636 RELATED-TO UniProt O84642 RELATED-TO 1 aromatic amino acid aminotransferase MetaCyc ENZRXN-14577 1 Additional kinetic data pertaining to tyrosine, p-hydroxyphenylpyruvate, and oxaloacetate have been determined |CITS: [236311][15983]|. 1 REVERSIBLE tyrosine aminotransferase MetaCyc TYRAMINOTRANS-ENZRXN Tyrosine inhibits competitively with respect to prephenate, with a kI of 100 &micro;M |CITS: [4929151][16269762][6338013]|. 1.3.1.12 1 1 Prephenate dehydrogenase 1 1 |FRAME: NAD| and |FRAME: NADP| are two forms of |FRAME: NIACINE|. These molecules are the biological carriers of reductive equivalents (i.e. high potential electrons). They are often referred to as coenzymes, although in most of their reactions they function as cosubstrates rather than true coenzymes. The most common function of NAD+ is to accept two electrons and a proton (a hidride ion) from a substrate that is being oxidized. This reduction converts NAD+ to |FRAME: NADH|, the reduced form. NADH then diffuses or is being transported to a terminal oxidase, where the electrons are passed on, regenerating the oxidized form. |FRAME: NADPH|, on the other hand, is mostly involved in biosynthetic reactions, where it serves as an electron donor. NADPH is formed by reduction of NADP+, which occurs by different mechanisms in different types of organisms. In photosynthetic organisms NADP+ is reduced by |FRAME: CPLX-84|. In heterotrophic organisms NADP+ is reduced by central metabolism processes such as the pentose phosphate pathway (see |FRAME: OXIDATIVEPENT-PWY|). 663.43 NADH CML <cml> <molecule id="NADH" title="NADH" dictRef="dictNADH"> <atomArray> <atom id="NADH-atom1" elementType="C" x2="23018.0" y2="-50634.0"/> <atom id="NADH-atom2" elementType="C" x2="61758.0" y2="-30301.0"/> <atom id="NADH-atom3" elementType="O" x2="5565.0" y2="-42962.0"/> <atom id="NADH-atom4" elementType="O" x2="5565.0" y2="-58112.0" formalCharge="-1"/> <atom id="NADH-atom5" elementType="C" x2="28771.0" y2="-62523.0"/> <atom id="NADH-atom6" elementType="C" x2="-39699.0" y2="-24166.0"/> <atom id="NADH-atom7" elementType="C" x2="-52742.0" y2="-29154.0"/> <atom id="NADH-atom8" elementType="O" x2="28771.0" y2="-67128.0"/> <atom id="NADH-atom9" elementType="C" x2="34906.0" y2="-31073.0"/> <atom id="NADH-atom10" elementType="C" x2="-67128.0" y2="-29154.0"/> <atom id="NADH-atom11" elementType="C" x2="-28388.0" y2="-45842.0"/> <atom id="NADH-atom12" elementType="C" x2="51782.0" y2="-30301.0"/> <atom id="NADH-atom13" elementType="O" x2="-37209.0" y2="-41042.0"/> <atom id="NADH-atom14" elementType="C" x2="43344.0" y2="-55622.0"/> <atom id="NADH-atom15" elementType="O" x2="-32799.0" y2="-56582.0"/> <atom id="NADH-atom16" elementType="C" x2="24931.0" y2="-55622.0"/> <atom id="NADH-atom17" elementType="C" x2="34906.0" y2="-40854.0"/> <atom id="NADH-atom18" elementType="C" x2="-32799.0" y2="-51977.0"/> <atom id="NADH-atom19" elementType="C" x2="-41425.0" y2="-51977.0"/> <atom id="NADH-atom20" elementType="O" x2="33564.0" y2="-50057.0"/> <atom id="NADH-atom21" elementType="N" x2="-60220.0" y2="-8821.0"/> <atom id="NADH-atom22" elementType="O" x2="14385.0" y2="-50634.0"/> <atom id="NADH-atom23" elementType="O" x2="-11888.0" y2="-42962.0"/> <atom id="NADH-atom24" elementType="N" x2="-67128.0" y2="-20904.0"/> <atom id="NADH-atom25" elementType="N" x2="-45647.0" y2="-32416.0"/> <atom id="NADH-atom26" elementType="N" x2="66745.0" y2="-35866.0"/> <atom id="NADH-atom27" elementType="C" x2="51782.0" y2="-40854.0"/> <atom id="NADH-atom28" elementType="C" x2="-52742.0" y2="-20904.0"/> <atom id="NADH-atom29" elementType="P" x2="5565.0" y2="-50634.0"/> <atom id="NADH-atom30" elementType="O" x2="-41425.0" y2="-56582.0"/> <atom id="NADH-atom31" elementType="N" x2="-45647.0" y2="-17259.0"/> <atom id="NADH-atom32" elementType="P" x2="-11888.0" y2="-50634.0"/> <atom id="NADH-atom33" elementType="C" x2="-45647.0" y2="-45842.0"/> <atom id="NADH-atom34" elementType="N" x2="43344.0" y2="-45452.0"/> <atom id="NADH-atom35" elementType="O" x2="66933.0" y2="-24931.0"/> <atom id="NADH-atom36" elementType="N" x2="-60220.0" y2="-32799.0"/> <atom id="NADH-atom37" elementType="C" x2="-24743.0" y2="-51400.0"/> <atom id="NADH-atom38" elementType="O" x2="38357.0" y2="-67128.0"/> <atom id="NADH-atom39" elementType="O" x2="-11888.0" y2="-58112.0" formalCharge="-1"/> <atom id="NADH-atom40" elementType="C" x2="-60220.0" y2="-16688.0"/> <atom id="NADH-atom41" elementType="O" x2="-18413.0" y2="-50634.0"/> <atom id="NADH-atom42" elementType="O" x2="-2880.0" y2="-50634.0"/> <atom id="NADH-atom43" elementType="C" x2="38357.0" y2="-62523.0"/> <atom id="NADH-atom44" elementType="C" x2="43922.0" y2="-26274.0"/> </atomArray> <bondArray> <bond id="NADH-bond1" atomRefs="NADH-atom44 NADH-atom12" order="1"/> <bond id="NADH-bond2" atomRefs="NADH-atom43 NADH-atom5" order="1"/> <bond id="NADH-bond3" atomRefs="NADH-atom42 NADH-atom32" order="1"/> <bond id="NADH-bond4" atomRefs="NADH-atom41 NADH-atom37" order="1"/> <bond id="NADH-bond5" atomRefs="NADH-atom40 NADH-atom24" order="1"/> <bond id="NADH-bond6" atomRefs="NADH-atom39 NADH-atom32" order="1"/> <bond id="NADH-bond7" atomRefs="NADH-atom38 NADH-atom43" order="1"/> <bond id="NADH-bond8" atomRefs="NADH-atom37 NADH-atom11" order="1"/> <bond id="NADH-bond9" atomRefs="NADH-atom36 NADH-atom7" order="2"/> <bond id="NADH-bond10" atomRefs="NADH-atom35 NADH-atom2" order="2"/> <bond id="NADH-bond11" atomRefs="NADH-atom34 NADH-atom14" order="1"/> <bond id="NADH-bond12" atomRefs="NADH-atom34 NADH-atom17" order="1"/> <bond id="NADH-bond13" atomRefs="NADH-atom33 NADH-atom25" order="1"/> <bond id="NADH-bond14" atomRefs="NADH-atom33 NADH-atom19" order="1"/> <bond id="NADH-bond15" atomRefs="NADH-atom32 NADH-atom41" order="1"/> <bond id="NADH-bond16" atomRefs="NADH-atom31 NADH-atom28" order="1"/> <bond id="NADH-bond17" atomRefs="NADH-atom30 NADH-atom19" order="1"/> <bond id="NADH-bond18" atomRefs="NADH-atom29 NADH-atom42" order="1"/> <bond id="NADH-bond19" atomRefs="NADH-atom28 NADH-atom40" order="2"/> <bond id="NADH-bond20" atomRefs="NADH-atom28 NADH-atom7" order="1"/> <bond id="NADH-bond21" atomRefs="NADH-atom27 NADH-atom34" order="1"/> <bond id="NADH-bond22" atomRefs="NADH-atom26 NADH-atom2" order="1"/> <bond id="NADH-bond23" atomRefs="NADH-atom25 NADH-atom6" order="1"/> <bond id="NADH-bond24" atomRefs="NADH-atom24 NADH-atom10" order="2"/> <bond id="NADH-bond25" atomRefs="NADH-atom23 NADH-atom32" order="2"/> <bond id="NADH-bond26" atomRefs="NADH-atom22 NADH-atom29" order="1"/> <bond id="NADH-bond27" atomRefs="NADH-atom21 NADH-atom40" order="1"/> <bond id="NADH-bond28" atomRefs="NADH-atom20 NADH-atom16" order="1"/> <bond id="NADH-bond29" atomRefs="NADH-atom18 NADH-atom19" order="1"/> <bond id="NADH-bond30" atomRefs="NADH-atom16 NADH-atom1" order="1"/> <bond id="NADH-bond31" atomRefs="NADH-atom16 NADH-atom5" order="1"/> <bond id="NADH-bond32" atomRefs="NADH-atom15 NADH-atom18" order="1"/> <bond id="NADH-bond33" atomRefs="NADH-atom14 NADH-atom20" order="1"/> <bond id="NADH-bond34" atomRefs="NADH-atom14 NADH-atom43" order="1"/> <bond id="NADH-bond35" atomRefs="NADH-atom13 NADH-atom33" order="1"/> <bond id="NADH-bond36" atomRefs="NADH-atom12 NADH-atom27" order="2"/> <bond id="NADH-bond37" atomRefs="NADH-atom11 NADH-atom13" order="1"/> <bond id="NADH-bond38" atomRefs="NADH-atom11 NADH-atom18" order="1"/> <bond id="NADH-bond39" atomRefs="NADH-atom10 NADH-atom36" order="1"/> <bond id="NADH-bond40" atomRefs="NADH-atom9 NADH-atom17" order="2"/> <bond id="NADH-bond41" atomRefs="NADH-atom9 NADH-atom44" order="1"/> <bond id="NADH-bond42" atomRefs="NADH-atom8 NADH-atom5" order="1"/> <bond id="NADH-bond43" atomRefs="NADH-atom7 NADH-atom25" order="1"/> <bond id="NADH-bond44" atomRefs="NADH-atom6 NADH-atom31" order="2"/> <bond id="NADH-bond45" atomRefs="NADH-atom4 NADH-atom29" order="1"/> <bond id="NADH-bond46" atomRefs="NADH-atom3 NADH-atom29" order="2"/> <bond id="NADH-bond47" atomRefs="NADH-atom2 NADH-atom12" order="1"/> <bond id="NADH-bond48" atomRefs="NADH-atom1 NADH-atom22" order="1"/> </bondArray> <formula concise="C 21 H 27 N 7 O 14 P 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">663.43</float> <string title="smiles">C(OP(=O)([O-])OP(=O)(OCC1(C(O)C(O)C(O1)N3(C2(C(=C(N)N=CN=2)N=C3))))[O-])C4(C(O)C(C(O4)N5(C=C(C(N)=O)CC=C5))O)</string> </molecule> </cml> NADH₂ NADH2 dihydrodiphosphopyridine nucleotide diphosphopyridine nucleotide reduced dihydronicotinamide adenine dinucleotide nicotinamide adenine dinucleotide reduced NAD-reduced NADH+H+ DPNH MetaCyc NADH LIGAND C00004 PubChem 439153 1 Hydroxyphenylpyruvate synthase MetaCyc PREPHENATEDEHYDROG-RXN UniProt P43901 UniProt Q02287 RELATED-TO UniProt Q04983 RELATED-TO UniProt P07023 RELATED-TO UniProt P43902 RELATED-TO UniProt Q9PIZ7 UniProt Q9CET9 1 prephenate dehydrogenase chorismate mutase-prephenate:NAD+ oxidoreductase(decarboxylating) chorismate mutase prephenate dehydrogenase MetaCyc PREPHENATEDEHYDROG-ENZRXN INHIBITION-COMPETITIVE 337.175 (6S)-6-fluoro-EPSP CML <cml> <molecule id="6S-6-FLUORO-EPSP" title="(6S)-6-fluoro-EPSP" dictRef="dict6S-6-FLUORO-EPSP"> <atomArray> <atom id="6S-6-FLUORO-EPSP-atom1" elementType="C" x2="0.0" y2="-1238.0"/> <atom id="6S-6-FLUORO-EPSP-atom2" elementType="C" x2="6129.0" y2="-523.0"/> <atom id="6S-6-FLUORO-EPSP-atom3" elementType="O" x2="4287.0" y2="-3712.0"/> <atom id="6S-6-FLUORO-EPSP-atom4" elementType="O" x2="1429.0" y2="-2062.0"/> <atom id="6S-6-FLUORO-EPSP-atom5" elementType="O" x2="6441.0" y2="-1631.0"/> <atom id="6S-6-FLUORO-EPSP-atom6" elementType="O" x2="714.0" y2="0.0" formalCharge="-1"/> <atom id="6S-6-FLUORO-EPSP-atom7" elementType="O" x2="2858.0" y2="-3712.0" formalCharge="-1"/> <atom id="6S-6-FLUORO-EPSP-atom8" elementType="O" x2="3572.0" y2="0.0"/> <atom id="6S-6-FLUORO-EPSP-atom9" elementType="O" x2="5304.0" y2="-1952.0" formalCharge="-1"/> <atom id="6S-6-FLUORO-EPSP-atom10" elementType="F" x2="2143.0" y2="-2475.0"/> <atom id="6S-6-FLUORO-EPSP-atom11" elementType="C" x2="4287.0" y2="-2062.0"/> <atom id="6S-6-FLUORO-EPSP-atom12" elementType="O" x2="2143.0" y2="-825.0"/> <atom id="6S-6-FLUORO-EPSP-atom13" elementType="O" x2="5001.0" y2="-825.0"/> <atom id="6S-6-FLUORO-EPSP-atom14" elementType="C" x2="714.0" y2="-825.0"/> <atom id="6S-6-FLUORO-EPSP-atom15" elementType="C" x2="3572.0" y2="-3300.0"/> <atom id="6S-6-FLUORO-EPSP-atom16" elementType="C" x2="1429.0" y2="-1238.0"/> <atom id="6S-6-FLUORO-EPSP-atom17" elementType="C" x2="3572.0" y2="-2475.0"/> <atom id="6S-6-FLUORO-EPSP-atom18" elementType="C" x2="3572.0" y2="-825.0"/> <atom id="6S-6-FLUORO-EPSP-atom19" elementType="C" x2="2858.0" y2="-2062.0"/> <atom id="6S-6-FLUORO-EPSP-atom20" elementType="C" x2="4287.0" y2="-1238.0"/> <atom id="6S-6-FLUORO-EPSP-atom21" elementType="C" x2="2858.0" y2="-1238.0"/> <atom id="6S-6-FLUORO-EPSP-atom22" elementType="P" x2="5716.0" y2="-1238.0"/> </atomArray> <bondArray> <bond id="6S-6-FLUORO-EPSP-bond1" atomRefs="6S-6-FLUORO-EPSP-atom21 6S-6-FLUORO-EPSP-atom19" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond2" atomRefs="6S-6-FLUORO-EPSP-atom21 6S-6-FLUORO-EPSP-atom18" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond3" atomRefs="6S-6-FLUORO-EPSP-atom20 6S-6-FLUORO-EPSP-atom18" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond4" atomRefs="6S-6-FLUORO-EPSP-atom19 6S-6-FLUORO-EPSP-atom17" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond5" atomRefs="6S-6-FLUORO-EPSP-atom15 6S-6-FLUORO-EPSP-atom17" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond6" atomRefs="6S-6-FLUORO-EPSP-atom14 6S-6-FLUORO-EPSP-atom16" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond7" atomRefs="6S-6-FLUORO-EPSP-atom13 6S-6-FLUORO-EPSP-atom22" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond8" atomRefs="6S-6-FLUORO-EPSP-atom20 6S-6-FLUORO-EPSP-atom13" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond9" atomRefs="6S-6-FLUORO-EPSP-atom21 6S-6-FLUORO-EPSP-atom12" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond10" atomRefs="6S-6-FLUORO-EPSP-atom12 6S-6-FLUORO-EPSP-atom16" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond11" atomRefs="6S-6-FLUORO-EPSP-atom20 6S-6-FLUORO-EPSP-atom11" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond12" atomRefs="6S-6-FLUORO-EPSP-atom11 6S-6-FLUORO-EPSP-atom17" order="2"/> <bond id="6S-6-FLUORO-EPSP-bond13" atomRefs="6S-6-FLUORO-EPSP-atom19 6S-6-FLUORO-EPSP-atom10" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond14" atomRefs="6S-6-FLUORO-EPSP-atom9 6S-6-FLUORO-EPSP-atom22" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond15" atomRefs="6S-6-FLUORO-EPSP-atom18 6S-6-FLUORO-EPSP-atom8" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond16" atomRefs="6S-6-FLUORO-EPSP-atom7 6S-6-FLUORO-EPSP-atom15" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond17" atomRefs="6S-6-FLUORO-EPSP-atom6 6S-6-FLUORO-EPSP-atom14" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond18" atomRefs="6S-6-FLUORO-EPSP-atom5 6S-6-FLUORO-EPSP-atom22" order="2"/> <bond id="6S-6-FLUORO-EPSP-bond19" atomRefs="6S-6-FLUORO-EPSP-atom4 6S-6-FLUORO-EPSP-atom16" order="2"/> <bond id="6S-6-FLUORO-EPSP-bond20" atomRefs="6S-6-FLUORO-EPSP-atom3 6S-6-FLUORO-EPSP-atom15" order="2"/> <bond id="6S-6-FLUORO-EPSP-bond21" atomRefs="6S-6-FLUORO-EPSP-atom2 6S-6-FLUORO-EPSP-atom22" order="1"/> <bond id="6S-6-FLUORO-EPSP-bond22" atomRefs="6S-6-FLUORO-EPSP-atom1 6S-6-FLUORO-EPSP-atom14" order="2"/> </bondArray> <formula concise="C 11 H 11 O 9 F 1 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">337.175</float> <string title="smiles">C=C([O-])C(=O)OC1(C(O)C(C=C(C(=O)[O-])C(F)1)OP(C)(=O)[O-])</string> </molecule> </cml> (6S)-6-fluoro-5-enolpyruvylshikimate-3-phosphate MetaCyc 6S-6-FLUORO-EPSP Bornemann S Ramjee MK Balasubramanian S Abell C Coggins JR Lowe DJ Thorneley RN PubMed 7559411 J Biol Chem 270(39);22811-5 Escherichia coli chorismate synthase catalyzes the conversion of (6S)-6-fluoro-5-enolpyruvylshikimate-3-phosphate to 6-fluorochorismate. Implications for the enzyme mechanism and the antimicrobial action of (6S)-6-fluoroshikimate. 1995 1 INHIBITION-COMPETITIVE 337.175 (6R)-6-fluoro-EPSP CML <cml> <molecule id="6R-6-FLUORO-EPSP" title="(6R)-6-fluoro-EPSP" dictRef="dict6R-6-FLUORO-EPSP"> <atomArray> <atom id="6R-6-FLUORO-EPSP-atom1" elementType="C" x2="0.0" y2="-1238.0"/> <atom id="6R-6-FLUORO-EPSP-atom2" elementType="C" x2="6129.0" y2="-523.0"/> <atom id="6R-6-FLUORO-EPSP-atom3" elementType="O" x2="4287.0" y2="-3712.0"/> <atom id="6R-6-FLUORO-EPSP-atom4" elementType="O" x2="1429.0" y2="-2062.0"/> <atom id="6R-6-FLUORO-EPSP-atom5" elementType="O" x2="6441.0" y2="-1631.0"/> <atom id="6R-6-FLUORO-EPSP-atom6" elementType="O" x2="714.0" y2="0.0" formalCharge="-1"/> <atom id="6R-6-FLUORO-EPSP-atom7" elementType="O" x2="2858.0" y2="-3712.0" formalCharge="-1"/> <atom id="6R-6-FLUORO-EPSP-atom8" elementType="O" x2="3572.0" y2="0.0"/> <atom id="6R-6-FLUORO-EPSP-atom9" elementType="O" x2="5304.0" y2="-1952.0" formalCharge="-1"/> <atom id="6R-6-FLUORO-EPSP-atom10" elementType="F" x2="2143.0" y2="-2475.0"/> <atom id="6R-6-FLUORO-EPSP-atom11" elementType="C" x2="4287.0" y2="-2062.0"/> <atom id="6R-6-FLUORO-EPSP-atom12" elementType="O" x2="2143.0" y2="-825.0"/> <atom id="6R-6-FLUORO-EPSP-atom13" elementType="O" x2="5001.0" y2="-825.0"/> <atom id="6R-6-FLUORO-EPSP-atom14" elementType="C" x2="714.0" y2="-825.0"/> <atom id="6R-6-FLUORO-EPSP-atom15" elementType="C" x2="3572.0" y2="-3300.0"/> <atom id="6R-6-FLUORO-EPSP-atom16" elementType="C" x2="1429.0" y2="-1238.0"/> <atom id="6R-6-FLUORO-EPSP-atom17" elementType="C" x2="3572.0" y2="-2475.0"/> <atom id="6R-6-FLUORO-EPSP-atom18" elementType="C" x2="3572.0" y2="-825.0"/> <atom id="6R-6-FLUORO-EPSP-atom19" elementType="C" x2="2858.0" y2="-2062.0"/> <atom id="6R-6-FLUORO-EPSP-atom20" elementType="C" x2="4287.0" y2="-1238.0"/> <atom id="6R-6-FLUORO-EPSP-atom21" elementType="C" x2="2858.0" y2="-1238.0"/> <atom id="6R-6-FLUORO-EPSP-atom22" elementType="P" x2="5716.0" y2="-1238.0"/> </atomArray> <bondArray> <bond id="6R-6-FLUORO-EPSP-bond1" atomRefs="6R-6-FLUORO-EPSP-atom21 6R-6-FLUORO-EPSP-atom19" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond2" atomRefs="6R-6-FLUORO-EPSP-atom21 6R-6-FLUORO-EPSP-atom18" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond3" atomRefs="6R-6-FLUORO-EPSP-atom20 6R-6-FLUORO-EPSP-atom18" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond4" atomRefs="6R-6-FLUORO-EPSP-atom19 6R-6-FLUORO-EPSP-atom17" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond5" atomRefs="6R-6-FLUORO-EPSP-atom15 6R-6-FLUORO-EPSP-atom17" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond6" atomRefs="6R-6-FLUORO-EPSP-atom14 6R-6-FLUORO-EPSP-atom16" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond7" atomRefs="6R-6-FLUORO-EPSP-atom13 6R-6-FLUORO-EPSP-atom22" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond8" atomRefs="6R-6-FLUORO-EPSP-atom20 6R-6-FLUORO-EPSP-atom13" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond9" atomRefs="6R-6-FLUORO-EPSP-atom21 6R-6-FLUORO-EPSP-atom12" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond10" atomRefs="6R-6-FLUORO-EPSP-atom12 6R-6-FLUORO-EPSP-atom16" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond11" atomRefs="6R-6-FLUORO-EPSP-atom20 6R-6-FLUORO-EPSP-atom11" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond12" atomRefs="6R-6-FLUORO-EPSP-atom11 6R-6-FLUORO-EPSP-atom17" order="2"/> <bond id="6R-6-FLUORO-EPSP-bond13" atomRefs="6R-6-FLUORO-EPSP-atom19 6R-6-FLUORO-EPSP-atom10" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond14" atomRefs="6R-6-FLUORO-EPSP-atom9 6R-6-FLUORO-EPSP-atom22" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond15" atomRefs="6R-6-FLUORO-EPSP-atom18 6R-6-FLUORO-EPSP-atom8" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond16" atomRefs="6R-6-FLUORO-EPSP-atom7 6R-6-FLUORO-EPSP-atom15" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond17" atomRefs="6R-6-FLUORO-EPSP-atom6 6R-6-FLUORO-EPSP-atom14" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond18" atomRefs="6R-6-FLUORO-EPSP-atom5 6R-6-FLUORO-EPSP-atom22" order="2"/> <bond id="6R-6-FLUORO-EPSP-bond19" atomRefs="6R-6-FLUORO-EPSP-atom4 6R-6-FLUORO-EPSP-atom16" order="2"/> <bond id="6R-6-FLUORO-EPSP-bond20" atomRefs="6R-6-FLUORO-EPSP-atom3 6R-6-FLUORO-EPSP-atom15" order="2"/> <bond id="6R-6-FLUORO-EPSP-bond21" atomRefs="6R-6-FLUORO-EPSP-atom2 6R-6-FLUORO-EPSP-atom22" order="1"/> <bond id="6R-6-FLUORO-EPSP-bond22" atomRefs="6R-6-FLUORO-EPSP-atom1 6R-6-FLUORO-EPSP-atom14" order="2"/> </bondArray> <formula concise="C 11 H 11 O 9 F 1 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">337.175</float> <string title="smiles">C=C([O-])C(=O)OC1(C(O)C(C=C(C(=O)[O-])C(F)1)OP(C)(=O)[O-])</string> </molecule> </cml> (6R)-6-fluoro-5-enolpyruvylshikimate 3-phosphate MetaCyc 6R-6-FLUORO-EPSP Osborne A Thorneley RN Abell C Bornemann S PubMed 10956653 J Biol Chem 275(46);35825-30 Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction. 2000 1 Glyphosate is a competive inhibitor with respect to PEP and a partial uncompetitive inhibitor with respect to shikimate 3-P. |CITS: [3111378] [7744055] [7589547]| INHIBITION-COMPETITIVE 167.058 glyphosate CML <cml> <molecule id="CPD0-1308" title="glyphosate" dictRef="dictCPD0-1308"> <atomArray> <atom id="CPD0-1308-atom1" elementType="P" x2="-25866.0" y2="-17093.0"/> <atom id="CPD0-1308-atom2" elementType="C" x2="-23731.0" y2="-25062.0"/> <atom id="CPD0-1308-atom3" elementType="N" x2="-15481.0" y2="-25062.0"/> <atom id="CPD0-1308-atom4" elementType="C" x2="-11356.0" y2="-32206.0"/> <atom id="CPD0-1308-atom5" elementType="C" x2="-3106.0" y2="-32206.0"/> <atom id="CPD0-1308-atom6" elementType="O" x2="1019.0" y2="-25062.0" formalCharge="-1"/> <atom id="CPD0-1308-atom7" elementType="O" x2="1019.0" y2="-39351.0"/> <atom id="CPD0-1308-atom8" elementType="O" x2="-33835.0" y2="-19228.0"/> <atom id="CPD0-1308-atom9" elementType="O" x2="-17897.0" y2="-14958.0" formalCharge="-1"/> <atom id="CPD0-1308-atom10" elementType="O" x2="-28001.0" y2="-9124.0"/> </atomArray> <bondArray> <bond id="CPD0-1308-bond1" atomRefs="CPD0-1308-atom1 CPD0-1308-atom2" order="1"/> <bond id="CPD0-1308-bond2" atomRefs="CPD0-1308-atom2 CPD0-1308-atom3" order="1"/> <bond id="CPD0-1308-bond3" atomRefs="CPD0-1308-atom3 CPD0-1308-atom4" order="1"/> <bond id="CPD0-1308-bond4" atomRefs="CPD0-1308-atom4 CPD0-1308-atom5" order="1"/> <bond id="CPD0-1308-bond5" atomRefs="CPD0-1308-atom5 CPD0-1308-atom6" order="1"/> <bond id="CPD0-1308-bond6" atomRefs="CPD0-1308-atom5 CPD0-1308-atom7" order="2"/> <bond id="CPD0-1308-bond7" atomRefs="CPD0-1308-atom1 CPD0-1308-atom8" order="2"/> <bond id="CPD0-1308-bond8" atomRefs="CPD0-1308-atom1 CPD0-1308-atom9" order="1"/> <bond id="CPD0-1308-bond9" atomRefs="CPD0-1308-atom1 CPD0-1308-atom10" order="1"/> </bondArray> <formula concise="C 3 H 6 N 1 O 5 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">167.058</float> <string title="smiles">C(C(=O)[O-])NCP(O)([O-])=O</string> </molecule> </cml> N-(phosphonomethyl)glycine MetaCyc CPD0-1308 ChEBI 27744 LIGAND C01705 1 Ammonium ions were the most effective activator. |CITS: [3111378]| ACTIVATION 6.941 Li+ CML <cml> <molecule id="LI+" title="Li+" dictRef="dictLI+"> <atomArray> <atom id="LI+-atom1" elementType="LI" x2="-640.0" y2="-999.0" formalCharge="1"/> </atomArray> <bondArray> </bondArray> <formula concise="LI 1" formalCharge="1"/> <float title="molecularWeight" units="g/mol">6.941</float> <string title="smiles">[Li+]</string> </molecule> </cml> lithium ion MetaCyc LI+ 1 Ammonium ions were the most effective activator. |CITS: [3111378]| ACTIVATION Cs+ cesium ion MetaCyc CPD-2 PubChem 104967 1 Ammonium ions were the most effective activator. |CITS: [3111378]| ACTIVATION 22.99 Na+ CML <cml> <molecule id="NA+" title="Na+" dictRef="dictNA+"> <atomArray> <atom id="NA+-atom1" elementType="NA" x2="-999.0" y2="-999.0" formalCharge="1"/> </atomArray> <bondArray> </bondArray> <formula concise="NA 1" formalCharge="1"/> <float title="molecularWeight" units="g/mol">22.99</float> <string title="smiles">[Na+]</string> </molecule> </cml> Sodium sodium ion MetaCyc NA+ LIGAND C01330 CAS 7440-23-5 1 Ammonium ions were the most effective activator. |CITS: [3111378]| ACTIVATION 85.47 Rb+ CML <cml> <molecule id="RB+" title="Rb+" dictRef="dictRB+"> <atomArray> <atom id="RB+-atom1" elementType="RB" x2="834.0" y2="-9990.0" formalCharge="1"/> </atomArray> <bondArray> </bondArray> <formula concise="RB 1" formalCharge="1"/> <float title="molecularWeight" units="g/mol">85.47</float> <string title="smiles">[Rb+]</string> </molecule> </cml> rubidium ion MetaCyc RB+ PubChem 105153 1 Ammonium ions were the most effective activator. |CITS: [3111378]| ACTIVATION 39.098 K+ CML <cml> <molecule id="K+" title="K+" dictRef="dictK+"> <atomArray> <atom id="K+-atom1" elementType="K" x2="-999.0" y2="-999.0" formalCharge="1"/> </atomArray> <bondArray> </bondArray> <formula concise="K 1" formalCharge="1"/> <float title="molecularWeight" units="g/mol">39.098</float> <string title="smiles">[K+]</string> </molecule> </cml> potassium potassium ion MetaCyc K+ LIGAND C00238 1 Ammonium ions were the most effective activator. |CITS: [3111378]| ACTIVATION 18.038 NH4+ CML <cml> <molecule id="AMMONIUM" title="NH4+" dictRef="dictAMMONIUM"> <atomArray> <atom id="AMMONIUM-atom1" elementType="H" x2="993990.0" y2="-3000.0"/> <atom id="AMMONIUM-atom2" elementType="H" x2="-3000.0" y2="-1000000.0"/> <atom id="AMMONIUM-atom3" elementType="N" x2="-3000.0" y2="-3000.0" formalCharge="1"/> <atom id="AMMONIUM-atom4" elementType="H" x2="-1000000.0" y2="-3000.0"/> <atom id="AMMONIUM-atom5" elementType="H" x2="-3000.0" y2="993990.0"/> </atomArray> <bondArray> <bond id="AMMONIUM-bond1" atomRefs="AMMONIUM-atom5 AMMONIUM-atom3" order="1"/> <bond id="AMMONIUM-bond2" atomRefs="AMMONIUM-atom4 AMMONIUM-atom3" order="1"/> <bond id="AMMONIUM-bond3" atomRefs="AMMONIUM-atom3 AMMONIUM-atom1" order="1"/> <bond id="AMMONIUM-bond4" atomRefs="AMMONIUM-atom3 AMMONIUM-atom2" order="1"/> </bondArray> <formula concise="H 4 N 1" formalCharge="1"/> <float title="molecularWeight" units="g/mol">18.038</float> <string title="smiles">[NH4+]</string> </molecule> </cml> ammonium MetaCyc AMMONIUM CAS 14798-03-9 LIGAND C01342 1 INHIBITION 165.951 3-bromopyruvate CML <cml> <molecule id="3-BROMOPYRUVATE" title="3-bromopyruvate" dictRef="dict3-BROMOPYRUVATE"> <atomArray> <atom id="3-BROMOPYRUVATE-atom1" elementType="O" x2="24236.0" y2="0.0"/> <atom id="3-BROMOPYRUVATE-atom2" elementType="O" x2="7746.0" y2="-576.0"/> <atom id="3-BROMOPYRUVATE-atom3" elementType="O" x2="24735.0" y2="-14280.0" formalCharge="-1"/> <atom id="3-BROMOPYRUVATE-atom4" elementType="BR" x2="0.0" y2="-15145.0"/> <atom id="3-BROMOPYRUVATE-atom5" elementType="C" x2="8245.0" y2="-14857.0"/> <atom id="3-BROMOPYRUVATE-atom6" elementType="C" x2="20363.0" y2="-7284.0"/> <atom id="3-BROMOPYRUVATE-atom7" elementType="C" x2="12118.0" y2="-7572.0"/> </atomArray> <bondArray> <bond id="3-BROMOPYRUVATE-bond1" atomRefs="3-BROMOPYRUVATE-atom6 3-BROMOPYRUVATE-atom7" order="1"/> <bond id="3-BROMOPYRUVATE-bond2" atomRefs="3-BROMOPYRUVATE-atom5 3-BROMOPYRUVATE-atom7" order="1"/> <bond id="3-BROMOPYRUVATE-bond3" atomRefs="3-BROMOPYRUVATE-atom4 3-BROMOPYRUVATE-atom5" order="1"/> <bond id="3-BROMOPYRUVATE-bond4" atomRefs="3-BROMOPYRUVATE-atom3 3-BROMOPYRUVATE-atom6" order="1"/> <bond id="3-BROMOPYRUVATE-bond5" atomRefs="3-BROMOPYRUVATE-atom2 3-BROMOPYRUVATE-atom7" order="2"/> <bond id="3-BROMOPYRUVATE-bond6" atomRefs="3-BROMOPYRUVATE-atom1 3-BROMOPYRUVATE-atom6" order="2"/> </bondArray> <formula concise="C 3 H 2 O 3 BR 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">165.951</float> <string title="smiles">C(Br)C(=O)C(=O)[O-]</string> </molecule> </cml> bromopyruvate 3-bromopyruvic acid bromopyruvic acid 3-bromo-2-oxopropanoic acid MetaCyc 3-BROMOPYRUVATE 1 Zollner, Helmward Weinheim, Federal Republic of Germany ; New York, NY, USA , 1989 Handbook of enzyme inhibitors Huynh QK PubMed 1899181 Arch Biochem Biophys 1991;284(2);407-12 5-Enolpyruvylshikimate-3-phosphate synthase from Escherichia coli--the substrate analogue bromopyruvate inactivates the enzyme by modifying Cys-408 and Lys-411. 1991 INHIBITION 1 INHIBITION 1 INHIBITION-COMPETITIVE 1 INHIBITION-ALLOSTERIC 1 Huang L Montoya AL Nester EW PubMed 170268 J Biol Chem 1975;250(19);7675-81 Purification and characterization of shikimate kinase enzyme activity in Bacillus subtilis. 1975 INHIBITION-ALLOSTERIC 1 Inhibition by EDTA can be reversed by addition of Mg<SUP>2+</SUP>. |CITS: [170268]| INHIBITION 289.221 EDTA CML <cml> <molecule id="EDTA" title="EDTA" dictRef="dictEDTA"> <atomArray> <atom id="EDTA-atom1" elementType="N" x2="4951.0" y2="-1650.0"/> <atom id="EDTA-atom2" elementType="C" x2="4951.0" y2="-825.0"/> <atom id="EDTA-atom3" elementType="C" x2="5665.0" y2="-2062.0"/> <atom id="EDTA-atom4" elementType="C" x2="4236.0" y2="-2062.0"/> <atom id="EDTA-atom5" elementType="C" x2="4236.0" y2="-412.0"/> <atom id="EDTA-atom6" elementType="C" x2="6380.0" y2="-1650.0"/> <atom id="EDTA-atom7" elementType="C" x2="3522.0" y2="-1650.0"/> <atom id="EDTA-atom8" elementType="N" x2="4236.0" y2="412.0" formalCharge="1"/> <atom id="EDTA-atom9" elementType="O" x2="7094.0" y2="-2062.0" formalCharge="-1"/> <atom id="EDTA-atom10" elementType="O" x2="6380.0" y2="-825.0"/> <atom id="EDTA-atom11" elementType="O" x2="2808.0" y2="-2062.0" formalCharge="-1"/> <atom id="EDTA-atom12" elementType="O" x2="3522.0" y2="-825.0"/> <atom id="EDTA-atom13" elementType="C" x2="3522.0" y2="825.0"/> <atom id="EDTA-atom14" elementType="C" x2="4951.0" y2="825.0"/> <atom id="EDTA-atom15" elementType="C" x2="2808.0" y2="412.0"/> <atom id="EDTA-atom16" elementType="C" x2="4951.0" y2="1650.0"/> <atom id="EDTA-atom17" elementType="O" x2="2093.0" y2="825.0" formalCharge="-1"/> <atom id="EDTA-atom18" elementType="O" x2="2808.0" y2="-412.0"/> <atom id="EDTA-atom19" elementType="O" x2="5665.0" y2="2062.0" formalCharge="-1"/> <atom id="EDTA-atom20" elementType="O" x2="4236.0" y2="2062.0"/> </atomArray> <bondArray> <bond id="EDTA-bond1" atomRefs="EDTA-atom16 EDTA-atom20" order="2"/> <bond id="EDTA-bond2" atomRefs="EDTA-atom16 EDTA-atom19" order="1"/> <bond id="EDTA-bond3" atomRefs="EDTA-atom15 EDTA-atom18" order="2"/> <bond id="EDTA-bond4" atomRefs="EDTA-atom15 EDTA-atom17" order="1"/> <bond id="EDTA-bond5" atomRefs="EDTA-atom14 EDTA-atom16" order="1"/> <bond id="EDTA-bond6" atomRefs="EDTA-atom13 EDTA-atom15" order="1"/> <bond id="EDTA-bond7" atomRefs="EDTA-atom8 EDTA-atom14" order="1"/> <bond id="EDTA-bond8" atomRefs="EDTA-atom8 EDTA-atom13" order="1"/> <bond id="EDTA-bond9" atomRefs="EDTA-atom7 EDTA-atom12" order="2"/> <bond id="EDTA-bond10" atomRefs="EDTA-atom7 EDTA-atom11" order="1"/> <bond id="EDTA-bond11" atomRefs="EDTA-atom6 EDTA-atom10" order="2"/> <bond id="EDTA-bond12" atomRefs="EDTA-atom6 EDTA-atom9" order="1"/> <bond id="EDTA-bond13" atomRefs="EDTA-atom5 EDTA-atom8" order="1"/> <bond id="EDTA-bond14" atomRefs="EDTA-atom4 EDTA-atom7" order="1"/> <bond id="EDTA-bond15" atomRefs="EDTA-atom3 EDTA-atom6" order="1"/> <bond id="EDTA-bond16" atomRefs="EDTA-atom2 EDTA-atom5" order="1"/> <bond id="EDTA-bond17" atomRefs="EDTA-atom1 EDTA-atom4" order="1"/> <bond id="EDTA-bond18" atomRefs="EDTA-atom1 EDTA-atom3" order="1"/> <bond id="EDTA-bond19" atomRefs="EDTA-atom1 EDTA-atom2" order="1"/> </bondArray> <formula concise="C 10 H 13 N 2 O 8" formalCharge="0"/> <float title="molecularWeight" units="g/mol">289.221</float> <string title="smiles">C(N(CC([O-])=O)CC([O-])=O)C[N+](CC([O-])=O)CC([O-])=O</string> </molecule> </cml> ethylenediaminetetraacetic acid ethylenediaminetetraacetate MetaCyc EDTA PubChem 6049 LIGAND C00284 1 Inhibition by p-hydroxymercuribenzoate is completely reversed by dithiothreitol. |CITS: [170268]| INHIBITION 337.705 p-hydroxymercuribenzoate CML <cml> <molecule id="P-HYDROXYMERCURIBENZOATE" title="p-hydroxymercuribenzoate" dictRef="dictP-HYDROXYMERCURIBENZOATE"> <atomArray> <atom id="P-HYDROXYMERCURIBENZOATE-atom1" elementType="O" x2="3572.0" y2="-2475.0"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom2" elementType="O" x2="0.0" y2="-412.0"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom3" elementType="O" x2="4287.0" y2="-1238.0" formalCharge="-1"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom4" elementType="C" x2="1429.0" y2="-1238.0"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom5" elementType="C" x2="2143.0" y2="0.0"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom6" elementType="C" x2="2143.0" y2="-1650.0"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom7" elementType="C" x2="2858.0" y2="-412.0"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom8" elementType="HG" x2="714.0" y2="0.0"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom9" elementType="C" x2="3572.0" y2="-1650.0"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom10" elementType="C" x2="1429.0" y2="-412.0"/> <atom id="P-HYDROXYMERCURIBENZOATE-atom11" elementType="C" x2="2858.0" y2="-1238.0"/> </atomArray> <bondArray> <bond id="P-HYDROXYMERCURIBENZOATE-bond1" atomRefs="P-HYDROXYMERCURIBENZOATE-atom9 P-HYDROXYMERCURIBENZOATE-atom11" order="1"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond2" atomRefs="P-HYDROXYMERCURIBENZOATE-atom8 P-HYDROXYMERCURIBENZOATE-atom10" order="1"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond3" atomRefs="P-HYDROXYMERCURIBENZOATE-atom11 P-HYDROXYMERCURIBENZOATE-atom7" order="1"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond4" atomRefs="P-HYDROXYMERCURIBENZOATE-atom6 P-HYDROXYMERCURIBENZOATE-atom11" order="2"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond5" atomRefs="P-HYDROXYMERCURIBENZOATE-atom5 P-HYDROXYMERCURIBENZOATE-atom10" order="1"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond6" atomRefs="P-HYDROXYMERCURIBENZOATE-atom7 P-HYDROXYMERCURIBENZOATE-atom5" order="2"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond7" atomRefs="P-HYDROXYMERCURIBENZOATE-atom10 P-HYDROXYMERCURIBENZOATE-atom4" order="2"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond8" atomRefs="P-HYDROXYMERCURIBENZOATE-atom4 P-HYDROXYMERCURIBENZOATE-atom6" order="1"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond9" atomRefs="P-HYDROXYMERCURIBENZOATE-atom3 P-HYDROXYMERCURIBENZOATE-atom9" order="1"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond10" atomRefs="P-HYDROXYMERCURIBENZOATE-atom2 P-HYDROXYMERCURIBENZOATE-atom8" order="1"/> <bond id="P-HYDROXYMERCURIBENZOATE-bond11" atomRefs="P-HYDROXYMERCURIBENZOATE-atom1 P-HYDROXYMERCURIBENZOATE-atom9" order="2"/> </bondArray> <formula concise="C 7 H 5 O 3 HG 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">337.705</float> <string title="smiles">C(=O)([O-])C1(=CC=C(C=C1)[Hg]O)</string> </molecule> </cml> p-hydroxymercuribenzoic acid (p-carboxyphenyl)hydroxymercury (4-carboxylatophenyl)hydroxymercurate(1-) hydrogen mercury, (p-carboxyphenyl)hydroxy- mercurate(1-), (4-carboxylateophenyl)hydroxy-, hydrogen (9Cl) MetaCyc P-HYDROXYMERCURIBENZOATE 1 INHIBITION 1 INHIBITION 1 INHIBITION 63.546 Cu2+ CML <cml> <molecule id="CU+2" title="Cu2+" dictRef="dictCU+2"> <atomArray> <atom id="CU+2-atom1" elementType="CU" x2="-952.0" y2="-999.0" formalCharge="2"/> </atomArray> <bondArray> </bondArray> <formula concise="CU 1" formalCharge="2"/> <float title="molecularWeight" units="g/mol">63.546</float> <string title="smiles">[Cu++]</string> </molecule> </cml> Cu<SUP>+2</SUP> Cu<SUP>++</SUP> cupric ion MetaCyc CU+2 1 Hasan N Nester EW PubMed 97286 J Biol Chem 1978;253(14);4999-5004 Dehydroquinate synthase in Bacillus subtilis. An enzyme associated with chorismate synthase and flavin reductase. 1978 INHIBITION 112.4 Cd2+ CML <cml> <molecule id="CD+2" title="Cd2+" dictRef="dictCD+2"> <atomArray> <atom id="CD+2-atom1" elementType="CD" x2="9990.0" y2="-2796.0" formalCharge="2"/> </atomArray> <bondArray> </bondArray> <formula concise="CD 1" formalCharge="2"/> <float title="molecularWeight" units="g/mol">112.4</float> <string title="smiles">[Cd++]</string> </molecule> </cml> Cadmium Cd<SUP>+2</SUP> Cd<SUP>++</SUP> MetaCyc CD+2 LIGAND C01413 PubChem 31193 1 NADH causes complete inhibition which is not reversed by addition of NAD. |CITS: [97286]| INHIBITION 1 INHIBITION 1 INHIBITION-COMPETITIVE 1 JAmChemSoc111-1861 INHIBITION-COMPETITIVE 269.124 alpha-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphate CML <cml> <molecule id="CPD0-1370" title="alpha-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphate"> <atomArray> <atom id="CPD0-1370-atom1" elementType="C" x2="2946.0" y2="-23571.0"/> <atom id="CPD0-1370-atom2" elementType="O" x2="-4198.0" y2="-19446.0"/> <atom id="CPD0-1370-atom3" elementType="C" x2="-4198.0" y2="-11196.0"/> <atom id="CPD0-1370-atom4" elementType="C" x2="2946.0" y2="-7071.0"/> <atom id="CPD0-1370-atom5" elementType="C" x2="10091.0" y2="-11196.0"/> <atom id="CPD0-1370-atom6" elementType="C" x2="10091.0" y2="-19446.0"/> <atom id="CPD0-1370-atom7" elementType="C" x2="8780.0" y2="-29404.0"/> <atom id="CPD0-1370-atom8" elementType="O" x2="6645.0" y2="-37373.0"/> <atom id="CPD0-1370-atom9" elementType="O" x2="16748.0" y2="-27269.0" formalCharge="-1"/> <atom id="CPD0-1370-atom10" elementType="O" x2="2946.0" y2="1179.0"/> <atom id="CPD0-1370-atom11" elementType="C" x2="-11343.0" y2="-7071.0"/> <atom id="CPD0-1370-atom12" elementType="O" x2="-11343.0" y2="1179.0"/> <atom id="CPD0-1370-atom13" elementType="P" x2="-11343.0" y2="9429.0"/> <atom id="CPD0-1370-atom14" elementType="O" x2="-4198.0" y2="13554.0" formalCharge="-1"/> <atom id="CPD0-1370-atom15" elementType="O" x2="-19592.0" y2="9429.0" formalCharge="-1"/> <atom id="CPD0-1370-atom16" elementType="O" x2="-11343.0" y2="17678.0"/> <atom id="CPD0-1370-atom17" elementType="O" x2="17235.0" y2="-7071.0"/> </atomArray> <bondArray> <bond id="CPD0-1370-bond1" atomRefs="CPD0-1370-atom1 CPD0-1370-atom2" order="1"/> <bond id="CPD0-1370-bond2" atomRefs="CPD0-1370-atom2 CPD0-1370-atom3" order="1"/> <bond id="CPD0-1370-bond3" atomRefs="CPD0-1370-atom3 CPD0-1370-atom4" order="1"/> <bond id="CPD0-1370-bond4" atomRefs="CPD0-1370-atom4 CPD0-1370-atom5" order="1"/> <bond id="CPD0-1370-bond5" atomRefs="CPD0-1370-atom5 CPD0-1370-atom6" order="1"/> <bond id="CPD0-1370-bond6" atomRefs="CPD0-1370-atom1 CPD0-1370-atom6" order="1"/> <bond id="CPD0-1370-bond7" atomRefs="CPD0-1370-atom7 CPD0-1370-atom1" order="1"/> <bond id="CPD0-1370-bond8" atomRefs="CPD0-1370-atom7 CPD0-1370-atom8" order="2"/> <bond id="CPD0-1370-bond9" atomRefs="CPD0-1370-atom7 CPD0-1370-atom9" order="1"/> <bond id="CPD0-1370-bond10" atomRefs="CPD0-1370-atom10 CPD0-1370-atom4" order="1"/> <bond id="CPD0-1370-bond11" atomRefs="CPD0-1370-atom3 CPD0-1370-atom11" order="1"/> <bond id="CPD0-1370-bond12" atomRefs="CPD0-1370-atom11 CPD0-1370-atom12" order="1"/> <bond id="CPD0-1370-bond13" atomRefs="CPD0-1370-atom12 CPD0-1370-atom13" order="1"/> <bond id="CPD0-1370-bond14" atomRefs="CPD0-1370-atom13 CPD0-1370-atom14" order="1"/> <bond id="CPD0-1370-bond15" atomRefs="CPD0-1370-atom13 CPD0-1370-atom15" order="1"/> <bond id="CPD0-1370-bond16" atomRefs="CPD0-1370-atom13 CPD0-1370-atom16" order="2"/> <bond id="CPD0-1370-bond17" atomRefs="CPD0-1370-atom5 CPD0-1370-atom17" order="1"/> </bondArray> <formula concise="C 7 H 10 O 9 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">269.124</float> <string title="smiles">C([O-])(=O)C1(CC(O)C(O)C(COP(=O)([O-])[O-])O1)</string> </molecule> </cml> MetaCyc CPD0-1370 1 INHIBITION-COMPETITIVE 257.157 alpha-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphonate CML <cml> <molecule id="CPD0-1372" title="alpha-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphonate"> <atomArray> <atom id="CPD0-1372-atom1" elementType="C" x2="-7955.0" y2="-19447.0"/> <atom id="CPD0-1372-atom2" elementType="O" x2="-15100.0" y2="-15322.0"/> <atom id="CPD0-1372-atom3" elementType="C" x2="-15100.0" y2="-7071.0"/> <atom id="CPD0-1372-atom4" elementType="C" x2="-7955.0" y2="-2946.0"/> <atom id="CPD0-1372-atom5" elementType="C" x2="-811.0" y2="-7071.0"/> <atom id="CPD0-1372-atom6" elementType="C" x2="-811.0" y2="-15322.0"/> <atom id="CPD0-1372-atom7" elementType="C" x2="-811.0" y2="-23572.0"/> <atom id="CPD0-1372-atom8" elementType="O" x2="-811.0" y2="-31822.0"/> <atom id="CPD0-1372-atom9" elementType="O" x2="7158.0" y2="-21436.0"/> <atom id="CPD0-1372-atom10" elementType="O" x2="6334.0" y2="-2946.0"/> <atom id="CPD0-1372-atom11" elementType="O" x2="-7955.0" y2="5304.0"/> <atom id="CPD0-1372-atom12" elementType="C" x2="-22245.0" y2="-2946.0"/> <atom id="CPD0-1372-atom13" elementType="P" x2="-22245.0" y2="5304.0"/> <atom id="CPD0-1372-atom14" elementType="O" x2="-30495.0" y2="5304.0" formalCharge="-1"/> <atom id="CPD0-1372-atom15" elementType="O" x2="-15100.0" y2="9429.0"/> <atom id="CPD0-1372-atom16" elementType="O" x2="-22245.0" y2="13554.0"/> </atomArray> <bondArray> <bond id="CPD0-1372-bond1" atomRefs="CPD0-1372-atom1 CPD0-1372-atom2" order="1"/> <bond id="CPD0-1372-bond2" atomRefs="CPD0-1372-atom2 CPD0-1372-atom3" order="1"/> <bond id="CPD0-1372-bond3" atomRefs="CPD0-1372-atom3 CPD0-1372-atom4" order="1"/> <bond id="CPD0-1372-bond4" atomRefs="CPD0-1372-atom4 CPD0-1372-atom5" order="1"/> <bond id="CPD0-1372-bond5" atomRefs="CPD0-1372-atom5 CPD0-1372-atom6" order="1"/> <bond id="CPD0-1372-bond6" atomRefs="CPD0-1372-atom1 CPD0-1372-atom6" order="1"/> <bond id="CPD0-1372-bond7" atomRefs="CPD0-1372-atom7 CPD0-1372-atom1" order="1"/> <bond id="CPD0-1372-bond8" atomRefs="CPD0-1372-atom7 CPD0-1372-atom8" order="1"/> <bond id="CPD0-1372-bond9" atomRefs="CPD0-1372-atom7 CPD0-1372-atom9" order="1"/> <bond id="CPD0-1372-bond10" atomRefs="CPD0-1372-atom5 CPD0-1372-atom10" order="1"/> <bond id="CPD0-1372-bond11" atomRefs="CPD0-1372-atom11 CPD0-1372-atom4" order="1"/> <bond id="CPD0-1372-bond12" atomRefs="CPD0-1372-atom3 CPD0-1372-atom12" order="1"/> <bond id="CPD0-1372-bond13" atomRefs="CPD0-1372-atom12 CPD0-1372-atom13" order="1"/> <bond id="CPD0-1372-bond14" atomRefs="CPD0-1372-atom13 CPD0-1372-atom14" order="1"/> <bond id="CPD0-1372-bond15" atomRefs="CPD0-1372-atom13 CPD0-1372-atom15" order="1"/> <bond id="CPD0-1372-bond16" atomRefs="CPD0-1372-atom13 CPD0-1372-atom16" order="2"/> </bondArray> <formula concise="C 7 H 14 O 8 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">257.157</float> <string title="smiles">C(O)(O)C1(CC(O)C(O)C(CP(=O)(O)[O-])O1)</string> </molecule> </cml> MetaCyc CPD0-1372 1 INHIBITION-COMPETITIVE 269.124 beta-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphate CML <cml> <molecule id="CPD0-1373" title="beta-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphate"> <atomArray> <atom id="CPD0-1373-atom1" elementType="C" x2="-12670.0" y2="-14143.0"/> <atom id="CPD0-1373-atom2" elementType="O" x2="-19813.0" y2="-10018.0"/> <atom id="CPD0-1373-atom3" elementType="C" x2="-19813.0" y2="-1768.0"/> <atom id="CPD0-1373-atom4" elementType="C" x2="-12670.0" y2="2357.0"/> <atom id="CPD0-1373-atom5" elementType="C" x2="-5525.0" y2="-1768.0"/> <atom id="CPD0-1373-atom6" elementType="C" x2="-5525.0" y2="-10018.0"/> <atom id="CPD0-1373-atom7" elementType="C" x2="-6836.0" y2="-19976.0"/> <atom id="CPD0-1373-atom8" elementType="O" x2="-6836.0" y2="-28226.0"/> <atom id="CPD0-1373-atom9" elementType="O" x2="1133.0" y2="-17840.0" formalCharge="-1"/> <atom id="CPD0-1373-atom10" elementType="O" x2="1620.0" y2="2357.0"/> <atom id="CPD0-1373-atom11" elementType="O" x2="-12670.0" y2="10607.0"/> <atom id="CPD0-1373-atom12" elementType="C" x2="-26958.0" y2="2357.0"/> <atom id="CPD0-1373-atom13" elementType="O" x2="-26958.0" y2="10607.0"/> <atom id="CPD0-1373-atom14" elementType="P" x2="-22833.0" y2="17751.0"/> <atom id="CPD0-1373-atom15" elementType="O" x2="-14865.0" y2="15617.0" formalCharge="-1"/> <atom id="CPD0-1373-atom16" elementType="O" x2="-30802.0" y2="19886.0" formalCharge="-1"/> <atom id="CPD0-1373-atom17" elementType="O" x2="-18708.0" y2="24896.0"/> </atomArray> <bondArray> <bond id="CPD0-1373-bond1" atomRefs="CPD0-1373-atom1 CPD0-1373-atom2" order="1"/> <bond id="CPD0-1373-bond2" atomRefs="CPD0-1373-atom2 CPD0-1373-atom3" order="1"/> <bond id="CPD0-1373-bond3" atomRefs="CPD0-1373-atom3 CPD0-1373-atom4" order="1"/> <bond id="CPD0-1373-bond4" atomRefs="CPD0-1373-atom4 CPD0-1373-atom5" order="1"/> <bond id="CPD0-1373-bond5" atomRefs="CPD0-1373-atom5 CPD0-1373-atom6" order="1"/> <bond id="CPD0-1373-bond6" atomRefs="CPD0-1373-atom1 CPD0-1373-atom6" order="1"/> <bond id="CPD0-1373-bond7" atomRefs="CPD0-1373-atom1 CPD0-1373-atom7" order="1"/> <bond id="CPD0-1373-bond8" atomRefs="CPD0-1373-atom7 CPD0-1373-atom8" order="2"/> <bond id="CPD0-1373-bond9" atomRefs="CPD0-1373-atom7 CPD0-1373-atom9" order="1"/> <bond id="CPD0-1373-bond10" atomRefs="CPD0-1373-atom5 CPD0-1373-atom10" order="1"/> <bond id="CPD0-1373-bond11" atomRefs="CPD0-1373-atom11 CPD0-1373-atom4" order="1"/> <bond id="CPD0-1373-bond12" atomRefs="CPD0-1373-atom3 CPD0-1373-atom12" order="1"/> <bond id="CPD0-1373-bond13" atomRefs="CPD0-1373-atom12 CPD0-1373-atom13" order="1"/> <bond id="CPD0-1373-bond14" atomRefs="CPD0-1373-atom13 CPD0-1373-atom14" order="1"/> <bond id="CPD0-1373-bond15" atomRefs="CPD0-1373-atom14 CPD0-1373-atom15" order="1"/> <bond id="CPD0-1373-bond16" atomRefs="CPD0-1373-atom14 CPD0-1373-atom16" order="1"/> <bond id="CPD0-1373-bond17" atomRefs="CPD0-1373-atom14 CPD0-1373-atom17" order="2"/> </bondArray> <formula concise="C 7 H 10 O 9 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">269.124</float> <string title="smiles">C([O-])(=O)C1(CC(O)C(O)C(COP(=O)([O-])[O-])O1)</string> </molecule> </cml> MetaCyc CPD0-1373 1 INHIBITION DAHP-o-methyl glycoside MetaCyc CPD0-1374 1 INHIBITION a oxygen substituted quinate MetaCyc Oxygen-Substituted-Quinates 1 INHIBITION-ALLOSTERIC 1 Huang L Montoya AL Nester EW PubMed 4210506 J Biol Chem 1974;249(14);4473-0 Characterization of the functional activities of the subunits of 3-deoxy-D-arabinoheptulosonate 7-phosphate synthetase-chorismate mutase from Bacillus subtilis 168. 1974 Huang L Nakatsukasa M Nester E PubMed 4211044 J Biol Chem 1974;249(14);4467-72 Regulation of aromatic amino acid biosynthesis in Bacillus subtilis 168. Purification, characterization, and subunit structure of the bifunctional enzyme 3-deoxy-D-arabinoheptulosonate 7-phosphate synthetase-chorismate mutase. 1974 Llewellyn DJ Daday A Smith GD PubMed 6101597 J Biol Chem 1980;255(5);2077-84 Evidence for an artificially evolved bifunctional 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase-chorismate mutase in Bacillus subtilis. 1980 Nester EW Lorence JH Nasser DS PubMed 4962501 Biochemistry 1967;6(5);1553-63 An enzyme aggregate involved in the biosynthesis of aromatic amino acids in Bacillus subtilis. Its possible function in feedback regulation. 1967 JMB12-468 INHIBITION-ALLOSTERIC 1 INHIBITION 1 INHIBITION 1 INHIBITION 1 The concentration of Co<SUP>2+</SUP> needed for enzyme stimulation is quite high so it may not be physiologically relevant. |CITS: [4211044]| ACTIVATION 1 ACTIVATION 1 INHIBITION-COMPETITIVE 1 INHIBITION 1 INHIBITION 1 INHIBITION 1 ACTIVATION 1 INHIBITION-COMPETITIVE 183.034 2-phosphoglycerate CML <cml> <molecule id="2-PG" title="2-phosphoglycerate" dictRef="dict2-PG"> <atomArray> <atom id="2-PG-atom1" elementType="O" x2="2476.0" y2="-3322.0"/> <atom id="2-PG-atom2" elementType="O" x2="1240.0" y2="0.0"/> <atom id="2-PG-atom3" elementType="O" x2="0.0" y2="-3322.0"/> <atom id="2-PG-atom4" elementType="O" x2="2476.0" y2="-1892.0" formalCharge="-1"/> <atom id="2-PG-atom5" elementType="O" x2="421.0" y2="-901.0" formalCharge="-1"/> <atom id="2-PG-atom6" elementType="O" x2="2067.0" y2="-896.0" formalCharge="-1"/> <atom id="2-PG-atom7" elementType="C" x2="413.0" y2="-2606.0"/> <atom id="2-PG-atom8" elementType="O" x2="1238.0" y2="-1783.0"/> <atom id="2-PG-atom9" elementType="C" x2="2063.0" y2="-2606.0"/> <atom id="2-PG-atom10" elementType="C" x2="1238.0" y2="-2606.0"/> <atom id="2-PG-atom11" elementType="P" x2="1256.0" y2="-889.0"/> </atomArray> <bondArray> <bond id="2-PG-bond1" atomRefs="2-PG-atom9 2-PG-atom10" order="1"/> <bond id="2-PG-bond2" atomRefs="2-PG-atom8 2-PG-atom11" order="1"/> <bond id="2-PG-bond3" atomRefs="2-PG-atom10 2-PG-atom8" order="1"/> <bond id="2-PG-bond4" atomRefs="2-PG-atom7 2-PG-atom10" order="1"/> <bond id="2-PG-bond5" atomRefs="2-PG-atom6 2-PG-atom11" order="1"/> <bond id="2-PG-bond6" atomRefs="2-PG-atom5 2-PG-atom11" order="1"/> <bond id="2-PG-bond7" atomRefs="2-PG-atom4 2-PG-atom9" order="1"/> <bond id="2-PG-bond8" atomRefs="2-PG-atom3 2-PG-atom7" order="1"/> <bond id="2-PG-bond9" atomRefs="2-PG-atom2 2-PG-atom11" order="2"/> <bond id="2-PG-bond10" atomRefs="2-PG-atom1 2-PG-atom9" order="2"/> </bondArray> <formula concise="C 3 H 4 O 7 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">183.034</float> <string title="smiles">C(O)C(OP(=O)([O-])[O-])C(=O)[O-]</string> </molecule> </cml> 2-PGA phosphoglycerate 2-phosphoglyceric acid 2-PG 2-P-glycerate glycerate 2-phosphate 2-phospho-D-glycerate 2-P-D-glycerate D-Glycerate 2-phosphate MetaCyc 2-PG CAS 2553-59-5 LIGAND C00631 1 INHIBITION-COMPETITIVE 2 1 INHIBITION-COMPETITIVE 3-BISPHOSPHOGLYCERATE 1 INHIBITION-COMPETITIVE 3-METHYLPHOSPHOENOLPYRUVATE 1 INHIBITION-COMPETITIVE 3-PROPYLPHOSPHOENOLPYRUVATE 1 INHIBITION BETA-2-THIENYL-D 1 INHIBITION L-DIHYDROPHENYLALANINE 1 INHIBITION 1 INHIBITION 89.094 L-alanine CML <cml> <molecule id="L-ALPHA-ALANINE" title="L-alanine" dictRef="dictL-ALPHA-ALANINE"> <atomArray> <atom id="L-ALPHA-ALANINE-atom1" elementType="C" x2="1271.0" y2="1040.0"/> <atom id="L-ALPHA-ALANINE-atom2" elementType="C" x2="1205.0" y2="996.0"/> <atom id="L-ALPHA-ALANINE-atom3" elementType="C" x2="1343.0" y2="1000.0"/> <atom id="L-ALPHA-ALANINE-atom4" elementType="N" x2="1274.0" y2="1122.0" formalCharge="1"/> <atom id="L-ALPHA-ALANINE-atom5" elementType="O" x2="1133.0" y2="1036.0" formalCharge="-1"/> <atom id="L-ALPHA-ALANINE-atom6" elementType="O" x2="1201.0" y2="912.0"/> </atomArray> <bondArray> <bond id="L-ALPHA-ALANINE-bond1" atomRefs="L-ALPHA-ALANINE-atom1 L-ALPHA-ALANINE-atom2" order="1"/> <bond id="L-ALPHA-ALANINE-bond2" atomRefs="L-ALPHA-ALANINE-atom1 L-ALPHA-ALANINE-atom3" order="1"/> <bond id="L-ALPHA-ALANINE-bond3" atomRefs="L-ALPHA-ALANINE-atom1 L-ALPHA-ALANINE-atom4" order="1"/> <bond id="L-ALPHA-ALANINE-bond4" atomRefs="L-ALPHA-ALANINE-atom2 L-ALPHA-ALANINE-atom5" order="1"/> <bond id="L-ALPHA-ALANINE-bond5" atomRefs="L-ALPHA-ALANINE-atom2 L-ALPHA-ALANINE-atom6" order="2"/> </bondArray> <formula concise="C 3 H 7 N 1 O 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">89.094</float> <string title="smiles">C(=O)([O-])C([N+])C</string> </molecule> </cml> alanine L-&alpha;-alanine MetaCyc L-ALPHA-ALANINE CAS 56-41-7 LIGAND C00041 1 INHIBITION-COMPETITIVE 1 INHIBITION 1 MethEnzV-794 INHIBITION 351.249 rCdRP CML <cml> <molecule id="CPD0-1486" title="rCdRP" dictRef="dictCPD0-1486"> <atomArray> <atom id="CPD0-1486-atom1" elementType="C" x2="-13554.0" y2="-27401.0"/> <atom id="CPD0-1486-atom2" elementType="C" x2="-20698.0" y2="-23277.0"/> <atom id="CPD0-1486-atom3" elementType="C" x2="-20698.0" y2="-15027.0"/> <atom id="CPD0-1486-atom4" elementType="C" x2="-13554.0" y2="-10902.0"/> <atom id="CPD0-1486-atom5" elementType="C" x2="-6409.0" y2="-15027.0"/> <atom id="CPD0-1486-atom6" elementType="C" x2="-6409.0" y2="-23277.0"/> <atom id="CPD0-1486-atom7" elementType="N" x2="-13554.0" y2="-2652.0"/> <atom id="CPD0-1486-atom8" elementType="O" x2="7394.0" y2="-11328.0" formalCharge="-1"/> <atom id="CPD0-1486-atom9" elementType="C" x2="-19387.0" y2="3182.0"/> <atom id="CPD0-1486-atom10" elementType="C" x2="-25221.0" y2="12257.0"/> <atom id="CPD0-1486-atom11" elementType="C" x2="-39363.0" y2="13141.0"/> <atom id="CPD0-1486-atom12" elementType="O" x2="-39363.0" y2="21391.0"/> <atom id="CPD0-1486-atom13" elementType="C" x2="-47553.0" y2="5245.0"/> <atom id="CPD0-1486-atom14" elementType="C" x2="-55214.0" y2="-1311.0"/> <atom id="CPD0-1486-atom15" elementType="O" x2="-41720.0" y2="-589.0"/> <atom id="CPD0-1486-atom16" elementType="O" x2="-63464.0" y2="-1311.0"/> <atom id="CPD0-1486-atom17" elementType="P" x2="-71714.0" y2="-1311.0"/> <atom id="CPD0-1486-atom18" elementType="O" x2="-71714.0" y2="-9561.0"/> <atom id="CPD0-1486-atom19" elementType="O" x2="-71714.0" y2="6939.0" formalCharge="-1"/> <atom id="CPD0-1486-atom20" elementType="O" x2="-79963.0" y2="-1311.0" formalCharge="-1"/> <atom id="CPD0-1486-atom21" elementType="O" x2="-25221.0" y2="20507.0"/> <atom id="CPD0-1486-atom22" elementType="C" x2="-575.0" y2="-9193.0"/> <atom id="CPD0-1486-atom23" elementType="O" x2="-2711.0" y2="-1224.0"/> </atomArray> <bondArray> <bond id="CPD0-1486-bond1" atomRefs="CPD0-1486-atom1 CPD0-1486-atom2" order="2"/> <bond id="CPD0-1486-bond2" atomRefs="CPD0-1486-atom2 CPD0-1486-atom3" order="1"/> <bond id="CPD0-1486-bond3" atomRefs="CPD0-1486-atom3 CPD0-1486-atom4" order="2"/> <bond id="CPD0-1486-bond4" atomRefs="CPD0-1486-atom4 CPD0-1486-atom5" order="1"/> <bond id="CPD0-1486-bond5" atomRefs="CPD0-1486-atom5 CPD0-1486-atom6" order="2"/> <bond id="CPD0-1486-bond6" atomRefs="CPD0-1486-atom1 CPD0-1486-atom6" order="1"/> <bond id="CPD0-1486-bond7" atomRefs="CPD0-1486-atom4 CPD0-1486-atom7" order="1"/> <bond id="CPD0-1486-bond8" atomRefs="CPD0-1486-atom5 CPD0-1486-atom22" order="1"/> <bond id="CPD0-1486-bond9" atomRefs="CPD0-1486-atom7 CPD0-1486-atom9" order="1"/> <bond id="CPD0-1486-bond10" atomRefs="CPD0-1486-atom9 CPD0-1486-atom10" order="1"/> <bond id="CPD0-1486-bond11" atomRefs="CPD0-1486-atom10 CPD0-1486-atom11" order="1"/> <bond id="CPD0-1486-bond12" atomRefs="CPD0-1486-atom11 CPD0-1486-atom12" order="1"/> <bond id="CPD0-1486-bond13" atomRefs="CPD0-1486-atom11 CPD0-1486-atom13" order="1"/> <bond id="CPD0-1486-bond14" atomRefs="CPD0-1486-atom13 CPD0-1486-atom14" order="1"/> <bond id="CPD0-1486-bond15" atomRefs="CPD0-1486-atom13 CPD0-1486-atom15" order="1"/> <bond id="CPD0-1486-bond16" atomRefs="CPD0-1486-atom14 CPD0-1486-atom16" order="1"/> <bond id="CPD0-1486-bond17" atomRefs="CPD0-1486-atom16 CPD0-1486-atom17" order="1"/> <bond id="CPD0-1486-bond18" atomRefs="CPD0-1486-atom17 CPD0-1486-atom18" order="2"/> <bond id="CPD0-1486-bond19" atomRefs="CPD0-1486-atom17 CPD0-1486-atom19" order="1"/> <bond id="CPD0-1486-bond20" atomRefs="CPD0-1486-atom17 CPD0-1486-atom20" order="1"/> <bond id="CPD0-1486-bond21" atomRefs="CPD0-1486-atom10 CPD0-1486-atom21" order="1"/> <bond id="CPD0-1486-bond22" atomRefs="CPD0-1486-atom8 CPD0-1486-atom22" order="1"/> <bond id="CPD0-1486-bond23" atomRefs="CPD0-1486-atom22 CPD0-1486-atom23" order="2"/> </bondArray> <formula concise="C 12 H 15 N 1 O 9 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">351.249</float> <string title="smiles">C(C(O)C(C(O)COP([O-])([O-])=O)O)NC1(C(C(=O)[O-])=CC=CC=1)</string> </molecule> </cml> reduced-1-[(2-carboxyphenyl)amino]-1-deoxyribulose 5-phosphate, MetaCyc CPD0-1486 1 Priestle JP Grutter MG White JL Vincent MG Kania M Wilson E Jardetzky TS Kirschner K Jansonius JN PubMed 3303031 Proc Natl Acad Sci U S A 1987;84(16);5690-4 Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli. 1987 INHIBITION 155.128 5-fluoroanthranilate CML <cml> <molecule id="CPD0-1487" title="5-fluoroanthranilate" dictRef="dictCPD0-1487"> <atomArray> <atom id="CPD0-1487-atom1" elementType="C" x2="-12375.0" y2="-7956.0"/> <atom id="CPD0-1487-atom2" elementType="C" x2="-19519.0" y2="-3830.0"/> <atom id="CPD0-1487-atom3" elementType="C" x2="-19519.0" y2="4420.0"/> <atom id="CPD0-1487-atom4" elementType="C" x2="-12375.0" y2="8545.0"/> <atom id="CPD0-1487-atom5" elementType="C" x2="-5230.0" y2="4420.0"/> <atom id="CPD0-1487-atom6" elementType="C" x2="-5230.0" y2="-3830.0"/> <atom id="CPD0-1487-atom7" elementType="F" x2="-12375.0" y2="-16206.0"/> <atom id="CPD0-1487-atom8" elementType="N" x2="-12375.0" y2="16794.0"/> <atom id="CPD0-1487-atom9" elementType="C" x2="1914.0" y2="8545.0"/> <atom id="CPD0-1487-atom10" elementType="O" x2="9059.0" y2="4420.0" formalCharge="-1"/> <atom id="CPD0-1487-atom11" elementType="O" x2="1914.0" y2="16794.0"/> </atomArray> <bondArray> <bond id="CPD0-1487-bond1" atomRefs="CPD0-1487-atom1 CPD0-1487-atom2" order="2"/> <bond id="CPD0-1487-bond2" atomRefs="CPD0-1487-atom2 CPD0-1487-atom3" order="1"/> <bond id="CPD0-1487-bond3" atomRefs="CPD0-1487-atom3 CPD0-1487-atom4" order="2"/> <bond id="CPD0-1487-bond4" atomRefs="CPD0-1487-atom4 CPD0-1487-atom5" order="1"/> <bond id="CPD0-1487-bond5" atomRefs="CPD0-1487-atom5 CPD0-1487-atom6" order="2"/> <bond id="CPD0-1487-bond6" atomRefs="CPD0-1487-atom1 CPD0-1487-atom6" order="1"/> <bond id="CPD0-1487-bond7" atomRefs="CPD0-1487-atom1 CPD0-1487-atom7" order="1"/> <bond id="CPD0-1487-bond8" atomRefs="CPD0-1487-atom4 CPD0-1487-atom8" order="1"/> <bond id="CPD0-1487-bond9" atomRefs="CPD0-1487-atom5 CPD0-1487-atom9" order="1"/> <bond id="CPD0-1487-bond10" atomRefs="CPD0-1487-atom9 CPD0-1487-atom10" order="1"/> <bond id="CPD0-1487-bond11" atomRefs="CPD0-1487-atom9 CPD0-1487-atom11" order="2"/> </bondArray> <formula concise="C 7 H 5 N 1 O 2 F 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">155.128</float> <string title="smiles">C(=O)([O-])C1(=CC(F)=CC=C(N)1)</string> </molecule> </cml> 5-fluoroanthranilic acid MetaCyc CPD0-1487 1 INHIBITION 151.165 5-methylanthranilate CML <cml> <molecule id="CPD0-1488" title="5-methylanthranilate" dictRef="dictCPD0-1488"> <atomArray> <atom id="CPD0-1488-atom1" elementType="C" x2="-10902.0" y2="-5304.0"/> <atom id="CPD0-1488-atom2" elementType="C" x2="-18045.0" y2="-1179.0"/> <atom id="CPD0-1488-atom3" elementType="C" x2="-18045.0" y2="7072.0"/> <atom id="CPD0-1488-atom4" elementType="C" x2="-10902.0" y2="11197.0"/> <atom id="CPD0-1488-atom5" elementType="C" x2="-3757.0" y2="7072.0"/> <atom id="CPD0-1488-atom6" elementType="C" x2="-3757.0" y2="-1179.0"/> <atom id="CPD0-1488-atom7" elementType="C" x2="-25190.0" y2="-5304.0"/> <atom id="CPD0-1488-atom8" elementType="C" x2="-10902.0" y2="19446.0"/> <atom id="CPD0-1488-atom9" elementType="O" x2="-18045.0" y2="23571.0" formalCharge="-1"/> <atom id="CPD0-1488-atom10" elementType="O" x2="-3757.0" y2="23571.0"/> <atom id="CPD0-1488-atom11" elementType="N" x2="3388.0" y2="11197.0"/> </atomArray> <bondArray> <bond id="CPD0-1488-bond1" atomRefs="CPD0-1488-atom1 CPD0-1488-atom2" order="2"/> <bond id="CPD0-1488-bond2" atomRefs="CPD0-1488-atom2 CPD0-1488-atom3" order="1"/> <bond id="CPD0-1488-bond3" atomRefs="CPD0-1488-atom3 CPD0-1488-atom4" order="2"/> <bond id="CPD0-1488-bond4" atomRefs="CPD0-1488-atom4 CPD0-1488-atom5" order="1"/> <bond id="CPD0-1488-bond5" atomRefs="CPD0-1488-atom5 CPD0-1488-atom6" order="2"/> <bond id="CPD0-1488-bond6" atomRefs="CPD0-1488-atom1 CPD0-1488-atom6" order="1"/> <bond id="CPD0-1488-bond7" atomRefs="CPD0-1488-atom2 CPD0-1488-atom7" order="1"/> <bond id="CPD0-1488-bond8" atomRefs="CPD0-1488-atom4 CPD0-1488-atom8" order="1"/> <bond id="CPD0-1488-bond9" atomRefs="CPD0-1488-atom8 CPD0-1488-atom9" order="1"/> <bond id="CPD0-1488-bond10" atomRefs="CPD0-1488-atom8 CPD0-1488-atom10" order="2"/> <bond id="CPD0-1488-bond11" atomRefs="CPD0-1488-atom5 CPD0-1488-atom11" order="1"/> </bondArray> <formula concise="C 8 H 8 N 1 O 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">151.165</float> <string title="smiles">CC1(C=C(C(=O)[O-])C(N)=CC=1)</string> </molecule> </cml> 5 - methylanthranilic acid MetaCyc CPD0-1488 1 INHIBITION 151.165 4-methylanthranilate CML <cml> <molecule id="CPD0-1489" title="4-methylanthranilate" dictRef="dictCPD0-1489"> <atomArray> <atom id="CPD0-1489-atom1" elementType="C" x2="-10902.0" y2="-5304.0"/> <atom id="CPD0-1489-atom2" elementType="C" x2="-18044.0" y2="-1179.0"/> <atom id="CPD0-1489-atom3" elementType="C" x2="-18044.0" y2="7072.0"/> <atom id="CPD0-1489-atom4" elementType="C" x2="-10902.0" y2="11197.0"/> <atom id="CPD0-1489-atom5" elementType="C" x2="-3757.0" y2="7072.0"/> <atom id="CPD0-1489-atom6" elementType="C" x2="-3757.0" y2="-1179.0"/> <atom id="CPD0-1489-atom7" elementType="C" x2="-10902.0" y2="19445.0"/> <atom id="CPD0-1489-atom8" elementType="O" x2="-18044.0" y2="23570.0" formalCharge="-1"/> <atom id="CPD0-1489-atom9" elementType="O" x2="-3757.0" y2="23570.0"/> <atom id="CPD0-1489-atom10" elementType="N" x2="3388.0" y2="11197.0"/> <atom id="CPD0-1489-atom11" elementType="C" x2="-10902.0" y2="-13554.0"/> </atomArray> <bondArray> <bond id="CPD0-1489-bond1" atomRefs="CPD0-1489-atom1 CPD0-1489-atom2" order="2"/> <bond id="CPD0-1489-bond2" atomRefs="CPD0-1489-atom2 CPD0-1489-atom3" order="1"/> <bond id="CPD0-1489-bond3" atomRefs="CPD0-1489-atom3 CPD0-1489-atom4" order="2"/> <bond id="CPD0-1489-bond4" atomRefs="CPD0-1489-atom4 CPD0-1489-atom5" order="1"/> <bond id="CPD0-1489-bond5" atomRefs="CPD0-1489-atom5 CPD0-1489-atom6" order="2"/> <bond id="CPD0-1489-bond6" atomRefs="CPD0-1489-atom1 CPD0-1489-atom6" order="1"/> <bond id="CPD0-1489-bond7" atomRefs="CPD0-1489-atom4 CPD0-1489-atom7" order="1"/> <bond id="CPD0-1489-bond8" atomRefs="CPD0-1489-atom7 CPD0-1489-atom8" order="1"/> <bond id="CPD0-1489-bond9" atomRefs="CPD0-1489-atom7 CPD0-1489-atom9" order="2"/> <bond id="CPD0-1489-bond10" atomRefs="CPD0-1489-atom5 CPD0-1489-atom10" order="1"/> <bond id="CPD0-1489-bond11" atomRefs="CPD0-1489-atom1 CPD0-1489-atom11" order="1"/> </bondArray> <formula concise="C 8 H 8 N 1 O 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">151.165</float> <string title="smiles">C(=O)([O-])C1(C(N)=CC(C)=CC=1)</string> </molecule> </cml> 4 - methylanthranilic acid MetaCyc CPD0-1489 1 INHIBITION 151.165 3-methylanthranilate CML <cml> <molecule id="CPD0-1490" title="3-methylanthranilate" dictRef="dictCPD0-1490"> <atomArray> <atom id="CPD0-1490-atom1" elementType="C" x2="-10902.0" y2="-5304.0"/> <atom id="CPD0-1490-atom2" elementType="C" x2="-18044.0" y2="-1179.0"/> <atom id="CPD0-1490-atom3" elementType="C" x2="-18044.0" y2="7072.0"/> <atom id="CPD0-1490-atom4" elementType="C" x2="-10902.0" y2="11197.0"/> <atom id="CPD0-1490-atom5" elementType="C" x2="-3757.0" y2="7072.0"/> <atom id="CPD0-1490-atom6" elementType="C" x2="-3757.0" y2="-1179.0"/> <atom id="CPD0-1490-atom7" elementType="C" x2="-10902.0" y2="19445.0"/> <atom id="CPD0-1490-atom8" elementType="O" x2="-18044.0" y2="23570.0" formalCharge="-1"/> <atom id="CPD0-1490-atom9" elementType="O" x2="-3757.0" y2="23570.0"/> <atom id="CPD0-1490-atom10" elementType="N" x2="3388.0" y2="11197.0"/> <atom id="CPD0-1490-atom11" elementType="C" x2="3388.0" y2="-5304.0"/> </atomArray> <bondArray> <bond id="CPD0-1490-bond1" atomRefs="CPD0-1490-atom1 CPD0-1490-atom2" order="2"/> <bond id="CPD0-1490-bond2" atomRefs="CPD0-1490-atom2 CPD0-1490-atom3" order="1"/> <bond id="CPD0-1490-bond3" atomRefs="CPD0-1490-atom3 CPD0-1490-atom4" order="2"/> <bond id="CPD0-1490-bond4" atomRefs="CPD0-1490-atom4 CPD0-1490-atom5" order="1"/> <bond id="CPD0-1490-bond5" atomRefs="CPD0-1490-atom5 CPD0-1490-atom6" order="2"/> <bond id="CPD0-1490-bond6" atomRefs="CPD0-1490-atom1 CPD0-1490-atom6" order="1"/> <bond id="CPD0-1490-bond7" atomRefs="CPD0-1490-atom4 CPD0-1490-atom7" order="1"/> <bond id="CPD0-1490-bond8" atomRefs="CPD0-1490-atom7 CPD0-1490-atom8" order="1"/> <bond id="CPD0-1490-bond9" atomRefs="CPD0-1490-atom7 CPD0-1490-atom9" order="2"/> <bond id="CPD0-1490-bond10" atomRefs="CPD0-1490-atom5 CPD0-1490-atom10" order="1"/> <bond id="CPD0-1490-bond11" atomRefs="CPD0-1490-atom6 CPD0-1490-atom11" order="1"/> </bondArray> <formula concise="C 8 H 8 N 1 O 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">151.165</float> <string title="smiles">C(=O)([O-])C1(C(N)=C(C)C=CC=1)</string> </molecule> </cml> 3 -methylanthranilic acid MetaCyc CPD0-1490 1 INHIBITION-COMPETITIVE 1 Competitive with respect to chorismate|CITS:[ItoCoxJBact9772569]| INHIBITION-COMPETITIVE 1 Baker TI Crawford IP PubMed 5333199 J Biol Chem 241(23);5577-84 Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli. 1966 Noncompetitive with respect to ammonium sulfate concentration INHIBITION-NONCOMPETITIVE 1 INHIBITION-COMPETITIVE 7-methyltryptophan 1 Held WA Smith OH PubMed 4904235 J Bacteriol 101(1);209-17 Mechanism of 3-methylanthranilic acid derepression of the tryptophan operon in Escherichia coli. 1970 Competitive with respect to tyrosine. |CITS: [11213]| INHIBITION-COMPETITIVE 1 INHIBITION-COMPETITIVE 1 Weigent DA Nester EW PubMed 11213 J Biol Chem 1976;251(22);6974-80 Purification and properties of two aromatic aminotransferases in Bacillus subtilis. 1976 INHIBITION-COMPETITIVE 1 INHIBITION-COMPETITIVE 220.144 L-histidinol-phosphate CML <cml> <molecule id="L-HISTIDINOL-P" title="L-histidinol-phosphate" dictRef="dictL-HISTIDINOL-P"> <atomArray> <atom id="L-HISTIDINOL-P-atom1" elementType="C" x2="1748.0" y2="-1220.0"/> <atom id="L-HISTIDINOL-P-atom2" elementType="C" x2="3129.0" y2="-1686.0"/> <atom id="L-HISTIDINOL-P-atom3" elementType="N" x2="2546.0" y2="-2501.0"/> <atom id="L-HISTIDINOL-P-atom4" elementType="C" x2="-457.0" y2="-2313.0"/> <atom id="L-HISTIDINOL-P-atom5" elementType="P" x2="-2313.0" y2="-2313.0"/> <atom id="L-HISTIDINOL-P-atom6" elementType="O" x2="-2313.0" y2="-1488.0"/> <atom id="L-HISTIDINOL-P-atom7" elementType="N" x2="332.0" y2="-1202.0" formalCharge="1"/> <atom id="L-HISTIDINOL-P-atom8" elementType="N" x2="2520.0" y2="-906.0"/> <atom id="L-HISTIDINOL-P-atom9" elementType="O" x2="-1533.0" y2="-2313.0"/> <atom id="L-HISTIDINOL-P-atom10" elementType="C" x2="1022.0" y2="-2367.0"/> <atom id="L-HISTIDINOL-P-atom11" elementType="O" x2="-2313.0" y2="-3138.0" formalCharge="-1"/> <atom id="L-HISTIDINOL-P-atom12" elementType="O" x2="-3138.0" y2="-2313.0" formalCharge="-1"/> <atom id="L-HISTIDINOL-P-atom13" elementType="C" x2="332.0" y2="-2026.0"/> <atom id="L-HISTIDINOL-P-atom14" elementType="C" x2="1748.0" y2="-2080.0"/> </atomArray> <bondArray> <bond id="L-HISTIDINOL-P-bond1" atomRefs="L-HISTIDINOL-P-atom14 L-HISTIDINOL-P-atom3" order="1"/> <bond id="L-HISTIDINOL-P-bond2" atomRefs="L-HISTIDINOL-P-atom14 L-HISTIDINOL-P-atom10" order="1"/> <bond id="L-HISTIDINOL-P-bond3" atomRefs="L-HISTIDINOL-P-atom13 L-HISTIDINOL-P-atom4" order="1"/> <bond id="L-HISTIDINOL-P-bond4" atomRefs="L-HISTIDINOL-P-atom12 L-HISTIDINOL-P-atom5" order="1"/> <bond id="L-HISTIDINOL-P-bond5" atomRefs="L-HISTIDINOL-P-atom11 L-HISTIDINOL-P-atom5" order="1"/> <bond id="L-HISTIDINOL-P-bond6" atomRefs="L-HISTIDINOL-P-atom10 L-HISTIDINOL-P-atom13" order="1"/> <bond id="L-HISTIDINOL-P-bond7" atomRefs="L-HISTIDINOL-P-atom9 L-HISTIDINOL-P-atom5" order="1"/> <bond id="L-HISTIDINOL-P-bond8" atomRefs="L-HISTIDINOL-P-atom8 L-HISTIDINOL-P-atom1" order="1"/> <bond id="L-HISTIDINOL-P-bond9" atomRefs="L-HISTIDINOL-P-atom7 L-HISTIDINOL-P-atom13" order="1"/> <bond id="L-HISTIDINOL-P-bond10" atomRefs="L-HISTIDINOL-P-atom6 L-HISTIDINOL-P-atom5" order="2"/> <bond id="L-HISTIDINOL-P-bond11" atomRefs="L-HISTIDINOL-P-atom4 L-HISTIDINOL-P-atom9" order="1"/> <bond id="L-HISTIDINOL-P-bond12" atomRefs="L-HISTIDINOL-P-atom3 L-HISTIDINOL-P-atom2" order="2"/> <bond id="L-HISTIDINOL-P-bond13" atomRefs="L-HISTIDINOL-P-atom2 L-HISTIDINOL-P-atom8" order="1"/> <bond id="L-HISTIDINOL-P-bond14" atomRefs="L-HISTIDINOL-P-atom1 L-HISTIDINOL-P-atom14" order="2"/> </bondArray> <formula concise="C 6 H 11 N 3 O 4 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">220.144</float> <string title="smiles">C1(=C(CC([N+])COP(=O)([O-])[O-])N=CN1)</string> </molecule> </cml> L-histidinol-phosphate histidinol-P L-histidinol-p histidinol-phosphate MetaCyc L-HISTIDINOL-P CAS 25679-93-0 LIGAND C01100 1 INHIBITION-COMPETITIVE 114.057 maleate CML <cml> <molecule id="MALEATE" title="maleate" dictRef="dictMALEATE"> <atomArray> <atom id="MALEATE-atom1" elementType="O" x2="-1979.0" y2="-4278.0" formalCharge="-1"/> <atom id="MALEATE-atom2" elementType="C" x2="-8661.0" y2="-8179.0"/> <atom id="MALEATE-atom3" elementType="O" x2="-8661.0" y2="15878.0"/> <atom id="MALEATE-atom4" elementType="C" x2="-15932.0" y2="-4598.0"/> <atom id="MALEATE-atom5" elementType="C" x2="-8661.0" y2="8127.0"/> <atom id="MALEATE-atom6" elementType="O" x2="-2352.0" y2="3636.0" formalCharge="-1"/> <atom id="MALEATE-atom7" elementType="C" x2="-15932.0" y2="3797.0"/> <atom id="MALEATE-atom8" elementType="O" x2="-8661.0" y2="-15932.0"/> </atomArray> <bondArray> <bond id="MALEATE-bond1" atomRefs="MALEATE-atom8 MALEATE-atom2" order="2"/> <bond id="MALEATE-bond2" atomRefs="MALEATE-atom7 MALEATE-atom4" order="2"/> <bond id="MALEATE-bond3" atomRefs="MALEATE-atom6 MALEATE-atom5" order="1"/> <bond id="MALEATE-bond4" atomRefs="MALEATE-atom5 MALEATE-atom7" order="1"/> <bond id="MALEATE-bond5" atomRefs="MALEATE-atom4 MALEATE-atom2" order="1"/> <bond id="MALEATE-bond6" atomRefs="MALEATE-atom3 MALEATE-atom5" order="2"/> <bond id="MALEATE-bond7" atomRefs="MALEATE-atom1 MALEATE-atom2" order="1"/> </bondArray> <formula concise="C 4 H 2 O 4" formalCharge="0"/> <float title="molecularWeight" units="g/mol">114.057</float> <string title="smiles">C([O-])(C=CC(=O)[O-])=O</string> </molecule> </cml> maleic acid cis-butenedioic acid MetaCyc MALEATE CAS 110-16-7 LIGAND C01384 1 Miyahara I Hirotsu K Hayashi H Kagamiyama H PubMed 7896726 J Biochem (Tokyo) 116(5);1001-12 X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms. 1994 INHIBITION-ALLOSTERIC 2-methylaspartate 1 Okamoto A Higuchi T Hirotsu K Kuramitsu S Kagamiyama H PubMed 7798192 J Biochem (Tokyo) 116(1);95-107 X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form. 1994 INHIBITION 115.108 2-keto-isovalerate CML <cml> <molecule id="2-KETO-ISOVALERATE" title="2-keto-isovalerate" dictRef="dict2-KETO-ISOVALERATE"> <atomArray> <atom id="2-KETO-ISOVALERATE-atom1" elementType="O" x2="73730.0" y2="-124730.0" formalCharge="-1"/> <atom id="2-KETO-ISOVALERATE-atom2" elementType="C" x2="-75210.0" y2="-124730.0"/> <atom id="2-KETO-ISOVALERATE-atom3" elementType="C" x2="-2720.0" y2="7900.0"/> <atom id="2-KETO-ISOVALERATE-atom4" elementType="O" x2="-2720.0" y2="90400.0"/> <atom id="2-KETO-ISOVALERATE-atom5" elementType="C" x2="-75210.0" y2="-42230.0"/> <atom id="2-KETO-ISOVALERATE-atom6" elementType="C" x2="-146660.0" y2="-980.0"/> <atom id="2-KETO-ISOVALERATE-atom7" elementType="C" x2="73730.0" y2="-42230.0"/> <atom id="2-KETO-ISOVALERATE-atom8" elementType="O" x2="145170.0" y2="-980.0"/> </atomArray> <bondArray> <bond id="2-KETO-ISOVALERATE-bond1" atomRefs="2-KETO-ISOVALERATE-atom7 2-KETO-ISOVALERATE-atom8" order="2"/> <bond id="2-KETO-ISOVALERATE-bond2" atomRefs="2-KETO-ISOVALERATE-atom5 2-KETO-ISOVALERATE-atom6" order="1"/> <bond id="2-KETO-ISOVALERATE-bond3" atomRefs="2-KETO-ISOVALERATE-atom3 2-KETO-ISOVALERATE-atom4" order="2"/> <bond id="2-KETO-ISOVALERATE-bond4" atomRefs="2-KETO-ISOVALERATE-atom5 2-KETO-ISOVALERATE-atom2" order="1"/> <bond id="2-KETO-ISOVALERATE-bond5" atomRefs="2-KETO-ISOVALERATE-atom7 2-KETO-ISOVALERATE-atom1" order="1"/> <bond id="2-KETO-ISOVALERATE-bond6" atomRefs="2-KETO-ISOVALERATE-atom5 2-KETO-ISOVALERATE-atom3" order="1"/> <bond id="2-KETO-ISOVALERATE-bond7" atomRefs="2-KETO-ISOVALERATE-atom7 2-KETO-ISOVALERATE-atom3" order="1"/> </bondArray> <formula concise="C 5 H 7 O 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">115.108</float> <string title="smiles">CC(C(C([O-])=O)=O)C</string> </molecule> </cml> 2-oxo-3-methylbutanoate 3-methyl-2-oxobutanoate &alpha;-keto-isovaleric acid &alpha;-ketoisopentanoic acid &alpha;-keto-isovalerate &alpha;-oxoisovalerate &alpha;-ketovaline 2-oxoisovalerate 2-ketovaline &alpha;-keto-valine 2-oxoisopentanoate 2-keto-3-methylbutyric acid MetaCyc 2-KETO-ISOVALERATE CAS 759-05-7 LIGAND C00141 1 Vartak NB Liu L Wang BM Berg CM PubMed 1646790 J Bacteriol 173(12);3864-71 A functional leuABCD operon is required for leucine synthesis by the tyrosine-repressible transaminase in Escherichia coli K-12. 1991 INHIBITION 131.174 L-leucine CML <cml> <molecule id="LEU" title="L-leucine" dictRef="dictLEU"> <atomArray> <atom id="LEU-atom1" elementType="C" x2="1475.0" y2="1142.0"/> <atom id="LEU-atom2" elementType="C" x2="1544.0" y2="1099.0"/> <atom id="LEU-atom3" elementType="C" x2="1402.0" y2="1103.0"/> <atom id="LEU-atom4" elementType="N" x2="1477.0" y2="1224.0" formalCharge="1"/> <atom id="LEU-atom5" elementType="C" x2="1616.0" y2="1138.0"/> <atom id="LEU-atom6" elementType="O" x2="1333.0" y2="1149.0" formalCharge="-1"/> <atom id="LEU-atom7" elementType="O" x2="1404.0" y2="1021.0"/> <atom id="LEU-atom8" elementType="C" x2="1686.0" y2="1094.0"/> <atom id="LEU-atom9" elementType="C" x2="1619.0" y2="1219.0"/> </atomArray> <bondArray> <bond id="LEU-bond1" atomRefs="LEU-atom1 LEU-atom2" order="1"/> <bond id="LEU-bond2" atomRefs="LEU-atom1 LEU-atom3" order="1"/> <bond id="LEU-bond3" atomRefs="LEU-atom4 LEU-atom1" order="1"/> <bond id="LEU-bond4" atomRefs="LEU-atom2 LEU-atom5" order="1"/> <bond id="LEU-bond5" atomRefs="LEU-atom3 LEU-atom6" order="1"/> <bond id="LEU-bond6" atomRefs="LEU-atom3 LEU-atom7" order="2"/> <bond id="LEU-bond7" atomRefs="LEU-atom5 LEU-atom8" order="1"/> <bond id="LEU-bond8" atomRefs="LEU-atom5 LEU-atom9" order="1"/> </bondArray> <formula concise="C 6 H 13 N 1 O 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">131.174</float> <string title="smiles">C(=O)([O-])C([N+])CC(C)C</string> </molecule> </cml> (2S)-&alpha;-2-amino-4-methylvaleric acid L leu leucine 2-amino-4-methylvaleric acid (2S)-&alpha;-leucine MetaCyc LEU CAS 61-90-5 NCI 46709 LIGAND C00123 1 Powell JT Morrison JF PubMed 361681 J Bacteriol 136(1);1-4 Role of the Escherichia coli aromatic amino acid aminotransferase in leucine biosynthesis. 1978 INHIBITION 1 Collier RH Kohlhaw G PubMed 4404056 J Bacteriol 1972;112(1);365-71 Nonidentity of the aspartate and the aromatic aminotransferase components of transaminase A in Escherichia coli. 1972 Competitive with respect to prephenate. |CITS: [4992710] [3110557] [104661] [114523]| INHIBITION-COMPETITIVE 1 Competitive with respect to prephenate. Tyrosine can reverse the inhibition but does not exhibit a strong allosteric effect alone. |CITS: [4992710] [114523] [104661] [3110557]| INHIBITION-COMPETITIVE 1 ACTIVATION-ALLOSTERIC 1 Fischer R Jensen R PubMed 3110557 Methods Enzymol 1987;142;507-12 Prephenate dehydratase (monofunctional). 1987 Riepl RG Glover GI PubMed 114523 J Biol Chem 1979;254(20);10321-8 Regulation and state of aggregation of Bacillus subtilis prephenate dehydratase in the presence of allosteric effectors. 1979 Riepl RG Glover GI PubMed 104661 Arch Biochem Biophys 1978;191(1);192-7 Purification of Prephenate dehydratase from Bacillus subtilis. 1978 Rebello JL Jensen RA PubMed 4992710 J Biol Chem 1970;245(15);3738-44 Metabolic interlock. The multi-metabolite control of prephenate dehydratase activity in Bacillus subtilis. 1970 ACTIVATION-ALLOSTERIC |FRAME: MET| (met) is an essential amino acid and is required for a number of important cellular functions, including the initiation of protein synthesis, the methylation of DNA, rRNA and xenobiotics, and the biosynthesis of cysteine, phospholipids and polyamines. 149.207 L-methionine CML <cml> <molecule id="MET" title="L-methionine" dictRef="dictMET"> <atomArray> <atom id="MET-atom1" elementType="C" x2="1443.0" y2="1144.0"/> <atom id="MET-atom2" elementType="C" x2="1376.0" y2="1100.0"/> <atom id="MET-atom3" elementType="C" x2="1515.0" y2="1104.0"/> <atom id="MET-atom4" elementType="N" x2="1446.0" y2="1227.0" formalCharge="1"/> <atom id="MET-atom5" elementType="O" x2="1303.0" y2="1140.0" formalCharge="-1"/> <atom id="MET-atom6" elementType="O" x2="1377.0" y2="1017.0"/> <atom id="MET-atom7" elementType="C" x2="1587.0" y2="1146.0"/> <atom id="MET-atom8" elementType="S" x2="1660.0" y2="1106.0"/> <atom id="MET-atom9" elementType="C" x2="1730.0" y2="1148.0"/> </atomArray> <bondArray> <bond id="MET-bond1" atomRefs="MET-atom1 MET-atom2" order="1"/> <bond id="MET-bond2" atomRefs="MET-atom1 MET-atom3" order="1"/> <bond id="MET-bond3" atomRefs="MET-atom4 MET-atom1" order="1"/> <bond id="MET-bond4" atomRefs="MET-atom2 MET-atom5" order="1"/> <bond id="MET-bond5" atomRefs="MET-atom2 MET-atom6" order="2"/> <bond id="MET-bond6" atomRefs="MET-atom3 MET-atom7" order="1"/> <bond id="MET-bond7" atomRefs="MET-atom7 MET-atom8" order="1"/> <bond id="MET-bond8" atomRefs="MET-atom8 MET-atom9" order="1"/> </bondArray> <formula concise="C 5 H 11 N 1 O 2 S 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">149.207</float> <string title="smiles">C(=O)([O-])C([N+])CCSC</string> </molecule> </cml> M met methionine MetaCyc MET CAS 63-68-3 LIGAND C00073 1 A modest, reversible, competitive inhibitor. INHIBITION-COMPETITIVE alpha-oxo-1-carboxy-5,6-dihydrothiopyranpropanoic acid 1 JOrgChem54-2404 A modest, reversible, competitive inhibitor. INHIBITION-COMPETITIVE alpha-oxo-1-carboxy-4-tetrahydrothiopyranpropanoic acid 1 INHIBITION-COMPETITIVE |FRAME: CIS-ACONITATE| is named after the plant |FRAME: TAX-112591|, from which it was first isolated in 1828 |CITS: [Peschier28]|. The plants of the genus Aconitum (family of the Ranunculaceae) are famous for the many alkaloids they contain |CITS: [Pictet04]|. 171.086 cis-aconitate CML <cml> <molecule id="CIS-ACONITATE" title="cis-aconitate" dictRef="dictCIS-ACONITATE"> <atomArray> <atom id="CIS-ACONITATE-atom1" elementType="O" x2="142380.0" y2="-89250.0"/> <atom id="CIS-ACONITATE-atom2" elementType="O" x2="-143080.0" y2="-89250.0"/> <atom id="CIS-ACONITATE-atom3" elementType="C" x2="-710.0" y2="-174250.0"/> <atom id="CIS-ACONITATE-atom4" elementType="C" x2="-143080.0" y2="-174250.0"/> <atom id="CIS-ACONITATE-atom5" elementType="C" x2="142380.0" y2="-174250.0"/> <atom id="CIS-ACONITATE-atom6" elementType="C" x2="70830.0" y2="-215330.0"/> <atom id="CIS-ACONITATE-atom7" elementType="O" x2="69420.0" y2="-37540.0" formalCharge="-1"/> <atom id="CIS-ACONITATE-atom8" elementType="O" x2="-64460.0" y2="-27630.0"/> <atom id="CIS-ACONITATE-atom9" elementType="C" x2="-710.0" y2="-85000.0"/> <atom id="CIS-ACONITATE-atom10" elementType="O" x2="-216750.0" y2="-216750.0" formalCharge="-1"/> <atom id="CIS-ACONITATE-atom11" elementType="O" x2="216040.0" y2="-216750.0" formalCharge="-1"/> <atom id="CIS-ACONITATE-atom12" elementType="C" x2="-72250.0" y2="-215330.0"/> </atomArray> <bondArray> <bond id="CIS-ACONITATE-bond1" atomRefs="CIS-ACONITATE-atom12 CIS-ACONITATE-atom3" order="1"/> <bond id="CIS-ACONITATE-bond2" atomRefs="CIS-ACONITATE-atom11 CIS-ACONITATE-atom5" order="1"/> <bond id="CIS-ACONITATE-bond3" atomRefs="CIS-ACONITATE-atom10 CIS-ACONITATE-atom4" order="1"/> <bond id="CIS-ACONITATE-bond4" atomRefs="CIS-ACONITATE-atom9 CIS-ACONITATE-atom3" order="1"/> <bond id="CIS-ACONITATE-bond5" atomRefs="CIS-ACONITATE-atom8 CIS-ACONITATE-atom9" order="2"/> <bond id="CIS-ACONITATE-bond6" atomRefs="CIS-ACONITATE-atom7 CIS-ACONITATE-atom9" order="1"/> <bond id="CIS-ACONITATE-bond7" atomRefs="CIS-ACONITATE-atom6 CIS-ACONITATE-atom3" order="2"/> <bond id="CIS-ACONITATE-bond8" atomRefs="CIS-ACONITATE-atom5 CIS-ACONITATE-atom6" order="1"/> <bond id="CIS-ACONITATE-bond9" atomRefs="CIS-ACONITATE-atom4 CIS-ACONITATE-atom12" order="1"/> <bond id="CIS-ACONITATE-bond10" atomRefs="CIS-ACONITATE-atom2 CIS-ACONITATE-atom4" order="2"/> <bond id="CIS-ACONITATE-bond11" atomRefs="CIS-ACONITATE-atom1 CIS-ACONITATE-atom5" order="2"/> </bondArray> <formula concise="C 6 H 3 O 6" formalCharge="0"/> <float title="molecularWeight" units="g/mol">171.086</float> <string title="smiles">C(=O)(CC(=CC(=O)[O-])C([O-])=O)[O-]</string> </molecule> </cml> MetaCyc CIS-ACONITATE CAS 585-84-2 LIGAND C00417 1 INHIBITION-COMPETITIVE 171.086 trans-aconitate CML <cml> <molecule id="CPD-225" title="trans-aconitate" dictRef="dictCPD-225"> <atomArray> <atom id="CPD-225-atom1" elementType="C" x2="16180.0" y2="-20395.0"/> <atom id="CPD-225-atom2" elementType="C" x2="16180.0" y2="-28645.0"/> <atom id="CPD-225-atom3" elementType="C" x2="23324.0" y2="-16270.0"/> <atom id="CPD-225-atom4" elementType="O" x2="30455.0" y2="-20418.0" formalCharge="-1"/> <atom id="CPD-225-atom5" elementType="O" x2="23297.0" y2="-8019.0"/> <atom id="CPD-225-atom6" elementType="C" x2="9034.0" y2="-32770.0"/> <atom id="CPD-225-atom7" elementType="O" x2="1905.0" y2="-28622.0" formalCharge="-1"/> <atom id="CPD-225-atom8" elementType="O" x2="9062.0" y2="-41021.0"/> <atom id="CPD-225-atom9" elementType="C" x2="23324.0" y2="-32770.0"/> <atom id="CPD-225-atom10" elementType="C" x2="23324.0" y2="-41020.0"/> <atom id="CPD-225-atom11" elementType="O" x2="16167.0" y2="-45121.0" formalCharge="-1"/> <atom id="CPD-225-atom12" elementType="O" x2="30483.0" y2="-45122.0"/> </atomArray> <bondArray> <bond id="CPD-225-bond1" atomRefs="CPD-225-atom9 CPD-225-atom10" order="1"/> <bond id="CPD-225-bond2" atomRefs="CPD-225-atom10 CPD-225-atom12" order="2"/> <bond id="CPD-225-bond3" atomRefs="CPD-225-atom10 CPD-225-atom11" order="1"/> <bond id="CPD-225-bond4" atomRefs="CPD-225-atom2 CPD-225-atom9" order="1"/> <bond id="CPD-225-bond5" atomRefs="CPD-225-atom2 CPD-225-atom6" order="1"/> <bond id="CPD-225-bond6" atomRefs="CPD-225-atom6 CPD-225-atom8" order="2"/> <bond id="CPD-225-bond7" atomRefs="CPD-225-atom6 CPD-225-atom7" order="1"/> <bond id="CPD-225-bond8" atomRefs="CPD-225-atom1 CPD-225-atom3" order="1"/> <bond id="CPD-225-bond9" atomRefs="CPD-225-atom3 CPD-225-atom5" order="2"/> <bond id="CPD-225-bond10" atomRefs="CPD-225-atom3 CPD-225-atom4" order="1"/> <bond id="CPD-225-bond11" atomRefs="CPD-225-atom1 CPD-225-atom2" order="2"/> </bondArray> <formula concise="C 6 H 3 O 6" formalCharge="0"/> <float title="molecularWeight" units="g/mol">171.086</float> <string title="smiles">C([O-])(=O)C=C(C([O-])=O)CC([O-])=O</string> </molecule> </cml> trans-aconitic acid MetaCyc CPD-225 CAS 4023-65-8 LIGAND C02341 1 INHIBITION-ALLOSTERIC 1 INHIBITION 196.033 tetranitromethane CML <cml> <molecule id="TETRANITROMETHANE" title="tetranitromethane" dictRef="dictTETRANITROMETHANE"> <atomArray> <atom id="TETRANITROMETHANE-atom1" elementType="C" x2="625.0" y2="2500.0"/> <atom id="TETRANITROMETHANE-atom2" elementType="N" x2="-7625.0" y2="2500.0"/> <atom id="TETRANITROMETHANE-atom3" elementType="N" x2="625.0" y2="-5750.0"/> <atom id="TETRANITROMETHANE-atom4" elementType="N" x2="8875.0" y2="2500.0"/> <atom id="TETRANITROMETHANE-atom5" elementType="N" x2="625.0" y2="10750.0"/> <atom id="TETRANITROMETHANE-atom6" elementType="O" x2="-6520.0" y2="-9875.0"/> <atom id="TETRANITROMETHANE-atom7" elementType="O" x2="7770.0" y2="-9875.0"/> <atom id="TETRANITROMETHANE-atom8" elementType="O" x2="13000.0" y2="-4645.0"/> <atom id="TETRANITROMETHANE-atom9" elementType="O" x2="13000.0" y2="9645.0"/> <atom id="TETRANITROMETHANE-atom10" elementType="O" x2="7770.0" y2="14875.0"/> <atom id="TETRANITROMETHANE-atom11" elementType="O" x2="-6520.0" y2="14875.0"/> <atom id="TETRANITROMETHANE-atom12" elementType="O" x2="-11750.0" y2="9645.0"/> <atom id="TETRANITROMETHANE-atom13" elementType="O" x2="-11750.0" y2="-4645.0"/> </atomArray> <bondArray> <bond id="TETRANITROMETHANE-bond1" atomRefs="TETRANITROMETHANE-atom2 TETRANITROMETHANE-atom12" order="2"/> <bond id="TETRANITROMETHANE-bond2" atomRefs="TETRANITROMETHANE-atom2 TETRANITROMETHANE-atom13" order="2"/> <bond id="TETRANITROMETHANE-bond3" atomRefs="TETRANITROMETHANE-atom5 TETRANITROMETHANE-atom11" order="2"/> <bond id="TETRANITROMETHANE-bond4" atomRefs="TETRANITROMETHANE-atom5 TETRANITROMETHANE-atom10" order="2"/> <bond id="TETRANITROMETHANE-bond5" atomRefs="TETRANITROMETHANE-atom4 TETRANITROMETHANE-atom9" order="2"/> <bond id="TETRANITROMETHANE-bond6" atomRefs="TETRANITROMETHANE-atom4 TETRANITROMETHANE-atom8" order="2"/> <bond id="TETRANITROMETHANE-bond7" atomRefs="TETRANITROMETHANE-atom3 TETRANITROMETHANE-atom7" order="2"/> <bond id="TETRANITROMETHANE-bond8" atomRefs="TETRANITROMETHANE-atom3 TETRANITROMETHANE-atom6" order="2"/> <bond id="TETRANITROMETHANE-bond9" atomRefs="TETRANITROMETHANE-atom1 TETRANITROMETHANE-atom4" order="1"/> <bond id="TETRANITROMETHANE-bond10" atomRefs="TETRANITROMETHANE-atom1 TETRANITROMETHANE-atom2" order="1"/> <bond id="TETRANITROMETHANE-bond11" atomRefs="TETRANITROMETHANE-atom1 TETRANITROMETHANE-atom5" order="1"/> <bond id="TETRANITROMETHANE-bond12" atomRefs="TETRANITROMETHANE-atom1 TETRANITROMETHANE-atom3" order="1"/> </bondArray> <formula concise="C 1 N 4 O 8" formalCharge="0"/> <float title="molecularWeight" units="g/mol">196.033</float> <string title="smiles">C(N(=O)=O)(N(=O)=O)(N(=O)=O)N(=O)=O</string> </molecule> </cml> MetaCyc TETRANITROMETHANE PubChem 10509 1 INHIBITION 1 INHIBITION 1 INHIBITION 1 Kane JF Stenmark SL Calhoun DH Jensen RA PubMed 4996881 J Biol Chem 1971;246(13);4308-16 Metabolic interlock. The role of the subordinate type of enzyme in the regulation of a complex pathway. 1971 INHIBITION-ALLOSTERIC 1 INHIBITION-ALLOSTERIC 1 ACTIVATION-ALLOSTERIC 1 INHIBITION-ALLOSTERIC 1 INHIBITION-ALLOSTERIC 1 ACTIVATION-ALLOSTERIC 1 INHIBITION 1 Hudson GS Howlett GJ Davidson BE PubMed 6338013 J Biol Chem 1983;258(5);3114-20 The binding of tyrosine and NAD+ to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self-association of the enzyme. Analysis in terms of a model. 1983 INHIBITION-COMPETITIVE 1 INHIBITION-COMPETITIVE 189.101 citrate CML <cml> <molecule id="CIT" title="citrate" dictRef="dictCIT"> <atomArray> <atom id="CIT-atom1" elementType="O" x2="-13517.0" y2="3794.0"/> <atom id="CIT-atom2" elementType="O" x2="13443.0" y2="4383.0"/> <atom id="CIT-atom3" elementType="O" x2="-21767.0" y2="-4457.0" formalCharge="-1"/> <atom id="CIT-atom4" elementType="C" x2="-479.0" y2="-9908.0"/> <atom id="CIT-atom5" elementType="C" x2="-13517.0" y2="-4457.0"/> <atom id="CIT-atom6" elementType="C" x2="-479.0" y2="-16685.0"/> <atom id="CIT-atom7" elementType="C" x2="-10423.0" y2="-9908.0"/> <atom id="CIT-atom8" elementType="O" x2="-479.0" y2="-1657.0"/> <atom id="CIT-atom9" elementType="O" x2="6077.0" y2="-21767.0"/> <atom id="CIT-atom10" elementType="C" x2="7919.0" y2="-9908.0"/> <atom id="CIT-atom11" elementType="O" x2="21694.0" y2="-3867.0" formalCharge="-1"/> <atom id="CIT-atom12" elementType="O" x2="-6961.0" y2="-21767.0" formalCharge="-1"/> <atom id="CIT-atom13" elementType="C" x2="13443.0" y2="-3867.0"/> </atomArray> <bondArray> <bond id="CIT-bond1" atomRefs="CIT-atom13 CIT-atom10" order="1"/> <bond id="CIT-bond2" atomRefs="CIT-atom12 CIT-atom6" order="1"/> <bond id="CIT-bond3" atomRefs="CIT-atom11 CIT-atom13" order="1"/> <bond id="CIT-bond4" atomRefs="CIT-atom10 CIT-atom4" order="1"/> <bond id="CIT-bond5" atomRefs="CIT-atom9 CIT-atom6" order="2"/> <bond id="CIT-bond6" atomRefs="CIT-atom8 CIT-atom4" order="1"/> <bond id="CIT-bond7" atomRefs="CIT-atom7 CIT-atom4" order="1"/> <bond id="CIT-bond8" atomRefs="CIT-atom6 CIT-atom4" order="1"/> <bond id="CIT-bond9" atomRefs="CIT-atom5 CIT-atom7" order="1"/> <bond id="CIT-bond10" atomRefs="CIT-atom3 CIT-atom5" order="1"/> <bond id="CIT-bond11" atomRefs="CIT-atom2 CIT-atom13" order="2"/> <bond id="CIT-bond12" atomRefs="CIT-atom1 CIT-atom5" order="2"/> </bondArray> <formula concise="C 6 H 5 O 7" formalCharge="0"/> <float title="molecularWeight" units="g/mol">189.101</float> <string title="smiles">C(=O)([O-])CC(C(=O)[O-])(O)CC(=O)[O-]</string> </molecule> </cml> citr cit citric acid 2-hydroxy-1,2,3-propanetricarboxylic acid MetaCyc CIT CAS 77-92-9 LIGAND C00158 1 INHIBITION-ALLOSTERIC 1 INHIBITION 213.106 246-trinitrobenzene CML <cml> <molecule id="246-TRINITROBENZENE" title="246-trinitrobenzene"> <atomArray> <atom id="246-TRINITROBENZENE-atom1" elementType="O" x2="0.0" y2="-2475.0"/> <atom id="246-TRINITROBENZENE-atom2" elementType="O" x2="714.0" y2="-3712.0"/> <atom id="246-TRINITROBENZENE-atom3" elementType="O" x2="2858.0" y2="0.0"/> <atom id="246-TRINITROBENZENE-atom4" elementType="O" x2="1429.0" y2="0.0"/> <atom id="246-TRINITROBENZENE-atom5" elementType="O" x2="3572.0" y2="-3712.0"/> <atom id="246-TRINITROBENZENE-atom6" elementType="O" x2="4287.0" y2="-2475.0"/> <atom id="246-TRINITROBENZENE-atom7" elementType="C" x2="1429.0" y2="-1650.0"/> <atom id="246-TRINITROBENZENE-atom8" elementType="C" x2="2143.0" y2="-2888.0"/> <atom id="246-TRINITROBENZENE-atom9" elementType="C" x2="2858.0" y2="-1650.0"/> <atom id="246-TRINITROBENZENE-atom10" elementType="C" x2="1429.0" y2="-2475.0"/> <atom id="246-TRINITROBENZENE-atom11" elementType="C" x2="2143.0" y2="-1238.0"/> <atom id="246-TRINITROBENZENE-atom12" elementType="C" x2="2858.0" y2="-2475.0"/> <atom id="246-TRINITROBENZENE-atom13" elementType="N" x2="714.0" y2="-2888.0"/> <atom id="246-TRINITROBENZENE-atom14" elementType="N" x2="2143.0" y2="-412.0"/> <atom id="246-TRINITROBENZENE-atom15" elementType="N" x2="3572.0" y2="-2888.0"/> </atomArray> <bondArray> <bond id="246-TRINITROBENZENE-bond1" atomRefs="246-TRINITROBENZENE-atom12 246-TRINITROBENZENE-atom15" order="1"/> <bond id="246-TRINITROBENZENE-bond2" atomRefs="246-TRINITROBENZENE-atom11 246-TRINITROBENZENE-atom14" order="1"/> <bond id="246-TRINITROBENZENE-bond3" atomRefs="246-TRINITROBENZENE-atom10 246-TRINITROBENZENE-atom13" order="1"/> <bond id="246-TRINITROBENZENE-bond4" atomRefs="246-TRINITROBENZENE-atom12 246-TRINITROBENZENE-atom9" order="2"/> <bond id="246-TRINITROBENZENE-bond5" atomRefs="246-TRINITROBENZENE-atom9 246-TRINITROBENZENE-atom11" order="1"/> <bond id="246-TRINITROBENZENE-bond6" atomRefs="246-TRINITROBENZENE-atom8 246-TRINITROBENZENE-atom12" order="1"/> <bond id="246-TRINITROBENZENE-bond7" atomRefs="246-TRINITROBENZENE-atom10 246-TRINITROBENZENE-atom8" order="2"/> <bond id="246-TRINITROBENZENE-bond8" atomRefs="246-TRINITROBENZENE-atom11 246-TRINITROBENZENE-atom7" order="2"/> <bond id="246-TRINITROBENZENE-bond9" atomRefs="246-TRINITROBENZENE-atom7 246-TRINITROBENZENE-atom10" order="1"/> <bond id="246-TRINITROBENZENE-bond10" atomRefs="246-TRINITROBENZENE-atom6 246-TRINITROBENZENE-atom15" order="2"/> <bond id="246-TRINITROBENZENE-bond11" atomRefs="246-TRINITROBENZENE-atom5 246-TRINITROBENZENE-atom15" order="2"/> <bond id="246-TRINITROBENZENE-bond12" atomRefs="246-TRINITROBENZENE-atom4 246-TRINITROBENZENE-atom14" order="2"/> <bond id="246-TRINITROBENZENE-bond13" atomRefs="246-TRINITROBENZENE-atom3 246-TRINITROBENZENE-atom14" order="2"/> <bond id="246-TRINITROBENZENE-bond14" atomRefs="246-TRINITROBENZENE-atom2 246-TRINITROBENZENE-atom13" order="2"/> <bond id="246-TRINITROBENZENE-bond15" atomRefs="246-TRINITROBENZENE-atom1 246-TRINITROBENZENE-atom13" order="2"/> </bondArray> <formula concise="C 6 H 3 N 3 O 6" formalCharge="0"/> <float title="molecularWeight" units="g/mol">213.106</float> <string title="smiles">C1(C(=CC(=CC=1N(=O)=O)N(=O)=O)N(=O)=O)</string> </molecule> </cml> MetaCyc 246-TRINITROBENZENE 1 INHIBITION L-2-HYDROXYGLUTARATE 1 INHIBITION 1 INHIBITION 1 INHIBITION 1 INHIBITION-COMPETITIVE 1 MetaCyc (http://biocyc.org) superpathway of phenylalanine, tyrosine, and tryptophan biosynthesis complete aromatic amino acid biosynthesis aromatic amino acid biosynthesis MetaCyc COMPLETE-ARO-PWY EcoCyc COMPLETE-ARO-PWY