90% of the activity present in the wild type strain is pfk-1. |CITS: [83294514]| The enzyme shows cooperative kinetics with the substrate fructose-6-phosphate but not with the other substrate ATP. |CITS: [85203917]| The reverse reaction does not participate in gluconeogenesis: fdp phosphatase mutants are deficient in gluconeogenesis.|CITS: [78194149]| Studies on phosphfructokinase-1 include subunit structure |CITS:[91255189]|, ligand binding |CITS: [91355204]| and pH dependence |CITS: [91255189]|. The allosteric properties of phosphofructokinase-1 are due in part to ligand binding and in part to the kinetics of the reaction. |CITS: [92144584]| PFK I Biochemistry 1989;28(17);6836-41 Bras GL PubMed Teschner W Urea-induced inactivation, dissociation, and unfolding of the allosteric phosphofructokinase from Escherichia coli. Deville-Bonne D Garel JR 2531001 1989 1828369 pH dependence of the kinetic properties of allosteric phosphofructokinase from Escherichia coli. Deville-Bonne D Bourgain F PubMed Biochemistry 1991;30(23);5750-4 Garel JR 1991 1.0 <cml> <molecule id="MG+2" title="Mg2+" dictRef="dictMG+2"> <atomArray> <atom id="MG+2-atom1" elementType="MG" x2="-1.0" y2="-1.0" formalCharge="2"/> </atomArray> <bondArray> </bondArray> <formula concise="MG 1" formalCharge="2"/> <float title="molecularWeight" units="g/mol">24.305</float> <string title="smiles">[Mg+2]</string> </molecule> </cml> CML 24.30500030517578 magnesium ion Mg<SUP>++</SUP> Mg2+ Mg<SUP>+2</SUP> Evans PR Rypniewski WR Crystal structure of unliganded phosphofructokinase from Escherichia coli. 1989 PubMed J Mol Biol 1989;207(4);805-21 2527305 Garel JR A conformational transition involved in antagonistic substrate binding to the allosteric phosphofructokinase from Escherichia coli. 1992 Deville-Bonne D Biochemistry 1992;31(6);1695-700 PubMed 1531298 2975709 Shirakihara Y J Mol Biol 1988;204(4);973-94 Evans PR 1988 Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products. PubMed 2140983 Role of the C-terminal region in the allosteric properties of Escherichia coli phosphofructokinase-1. Serre MC Eur J Biochem 1990;189(3);487-92 PubMed Garel JR 1990 6-phosphofructokinase-1 1991 Evans PR 1832014 Biochemistry 1991;30(34);8477-80 PubMed Steady-state fluorescence of Escherichia coli phosphofructokinase reveals a regulatory role for ATP. Berger SA This is a key control step in glycolysis |CITS: [79100775]| Biochemistry WH Freeman and Co., 3rd edition, New York, 1988 Stryer L fructose-6-phosphate phosphorylation 2.7.1.11 PubMed Uyeda K 153704 Phosphofructokinase. 1979 Adv Enzymol Relat Areas Mol Biol 1979;48;193-244 cytoplasm GO GO:0005737 CML <cml> <molecule id="ADP" title="ADP" dictRef="dictADP"> <atomArray> <atom id="ADP-atom1" elementType="C" x2="0.6623" y2="-0.17049"/> <atom id="ADP-atom2" elementType="N" x2="0.28197" y2="0.02295"/> <atom id="ADP-atom3" elementType="N" x2="0.46557" y2="-0.26885"/> <atom id="ADP-atom4" elementType="O" x2="-0.77705" y2="-0.78689"/> <atom id="ADP-atom5" elementType="O" x2="-0.36721" y2="-0.34098"/> <atom id="ADP-atom6" elementType="C" x2="0.46557" y2="-0.65902"/> <atom id="ADP-atom7" elementType="C" x2="0.22951" y2="-0.54426"/> <atom id="ADP-atom8" elementType="C" x2="0.87541" y2="-0.61967"/> <atom id="ADP-atom9" elementType="O" x2="-1.0" y2="-0.54426"/> <atom id="ADP-atom10" elementType="O" x2="-0.77705" y2="-0.34098"/> <atom id="ADP-atom11" elementType="O" x2="0.88525" y2="-0.97705"/> <atom id="ADP-atom12" elementType="P" x2="-0.36721" y2="-0.54426"/> <atom id="ADP-atom13" elementType="N" x2="0.46557" y2="0.34426"/> <atom id="ADP-atom14" elementType="N" x2="0.87541" y2="-0.21639"/> <atom id="ADP-atom15" elementType="P" x2="-0.77705" y2="-0.54426"/> <atom id="ADP-atom16" elementType="C" x2="0.99672" y2="-0.04262"/> <atom id="ADP-atom17" elementType="O" x2="0.53115" y2="-1.0"/> <atom id="ADP-atom18" elementType="O" x2="-0.57049" y2="-0.54426"/> <atom id="ADP-atom19" elementType="O" x2="-0.1541" y2="-0.54426"/> <atom id="ADP-atom20" elementType="C" x2="0.46557" y2="0.12131"/> <atom id="ADP-atom21" elementType="O" x2="0.65574" y2="-0.47541"/> <atom id="ADP-atom22" elementType="C" x2="0.6623" y2="0.02295"/> <atom id="ADP-atom23" elementType="C" x2="0.81311" y2="-0.86557"/> <atom id="ADP-atom24" elementType="H" x2="0.39344" y2="-0.77377"/> <atom id="ADP-atom25" elementType="N" x2="0.85246" y2="0.10492"/> <atom id="ADP-atom26" elementType="C" x2="0.28197" y2="-0.17049"/> <atom id="ADP-atom27" elementType="O" x2="-0.36721" y2="-0.78689"/> <atom id="ADP-atom28" elementType="C" x2="0.53115" y2="-0.86557"/> <atom id="ADP-atom29" elementType="H" x2="0.77377" y2="-0.7377"/> <atom id="ADP-atom30" elementType="H" x2="0.92459" y2="-0.74426"/> <atom id="ADP-atom31" elementType="H" x2="0.60328" y2="-0.75082"/> </atomArray> <bondArray> <bond id="ADP-bond1" atomRefs="ADP-atom31 ADP-atom28" order="1"/> <bond id="ADP-bond2" atomRefs="ADP-atom30 ADP-atom8" order="1"/> <bond id="ADP-bond3" atomRefs="ADP-atom29 ADP-atom23" order="1"/> <bond id="ADP-bond4" atomRefs="ADP-atom28 ADP-atom23" order="1"/> <bond id="ADP-bond5" atomRefs="ADP-atom27 ADP-atom12" order="1"/> <bond id="ADP-bond6" atomRefs="ADP-atom26 ADP-atom3" order="A"/> <bond id="ADP-bond7" atomRefs="ADP-atom25 ADP-atom16" order="A"/> <bond id="ADP-bond8" atomRefs="ADP-atom24 ADP-atom6" order="1"/> <bond id="ADP-bond9" atomRefs="ADP-atom1 ADP-atom22" order="A"/> <bond id="ADP-bond10" atomRefs="ADP-atom22 ADP-atom25" order="A"/> <bond id="ADP-bond11" atomRefs="ADP-atom21 ADP-atom8" order="1"/> <bond id="ADP-bond12" atomRefs="ADP-atom22 ADP-atom20" order="A"/> <bond id="ADP-bond13" atomRefs="ADP-atom19 ADP-atom7" order="1"/> <bond id="ADP-bond14" atomRefs="ADP-atom18 ADP-atom12" order="1"/> <bond id="ADP-bond15" atomRefs="ADP-atom17 ADP-atom28" order="1"/> <bond id="ADP-bond16" atomRefs="ADP-atom16 ADP-atom14" order="A"/> <bond id="ADP-bond17" atomRefs="ADP-atom15 ADP-atom18" order="1"/> <bond id="ADP-bond18" atomRefs="ADP-atom13 ADP-atom20" order="1"/> <bond id="ADP-bond19" atomRefs="ADP-atom12 ADP-atom19" order="1"/> <bond id="ADP-bond20" atomRefs="ADP-atom11 ADP-atom23" order="1"/> <bond id="ADP-bond21" atomRefs="ADP-atom10 ADP-atom15" order="2"/> <bond id="ADP-bond22" atomRefs="ADP-atom9 ADP-atom15" order="1"/> <bond id="ADP-bond23" atomRefs="ADP-atom8 ADP-atom14" order="1"/> <bond id="ADP-bond24" atomRefs="ADP-atom8 ADP-atom23" order="1"/> <bond id="ADP-bond25" atomRefs="ADP-atom7 ADP-atom6" order="1"/> <bond id="ADP-bond26" atomRefs="ADP-atom6 ADP-atom21" order="1"/> <bond id="ADP-bond27" atomRefs="ADP-atom6 ADP-atom28" order="1"/> <bond id="ADP-bond28" atomRefs="ADP-atom5 ADP-atom12" order="2"/> <bond id="ADP-bond29" atomRefs="ADP-atom4 ADP-atom15" order="1"/> <bond id="ADP-bond30" atomRefs="ADP-atom3 ADP-atom1" order="A"/> <bond id="ADP-bond31" atomRefs="ADP-atom2 ADP-atom26" order="A"/> <bond id="ADP-bond32" atomRefs="ADP-atom20 ADP-atom2" order="A"/> <bond id="ADP-bond33" atomRefs="ADP-atom14 ADP-atom1" order="A"/> </bondArray> <formula concise="C 10 H 15 N 5 O 10 P 2" formalCharge="-3"/> <float title="molecularWeight" units="g/mol">427.203</float> <string title="smiles">c12(n(cnc(c(N)ncn1)2)[CH]3(O[CH]([CH](O)[CH](O)3)COP(=O)(O)OP(O)(=O)O))</string> </molecule> </cml> adenosine-diphosphate CAS 58-64-0 adenosine 5'-pyrophosphate adenosine pyrophosphate ADP adenosine-5-diphosphate 427.2030029296875 adenosine-5'-diphosphate 1 1 260.1369934082031 <cml> <molecule id="FRUCTOSE-6P" title="fructose-6-phosphate" dictRef="dictFRUCTOSE-6P"> <atomArray> <atom id="FRUCTOSE-6P-atom1" elementType="O" x2="-0.41525424" y2="-0.3079096"/> <atom id="FRUCTOSE-6P-atom2" elementType="C" x2="-0.124293804" y2="-0.3079096"/> <atom id="FRUCTOSE-6P-atom3" elementType="H" x2="0.028248549" y2="-0.65254235"/> <atom id="FRUCTOSE-6P-atom4" elementType="C" x2="-0.124293804" y2="-0.519774"/> <atom id="FRUCTOSE-6P-atom5" elementType="H" x2="-0.124293804" y2="-0.6949153"/> <atom id="FRUCTOSE-6P-atom6" elementType="O" x2="0.6751412" y2="-0.279661"/> <atom id="FRUCTOSE-6P-atom7" elementType="O" x2="0.028248549" y2="-1.0"/> <atom id="FRUCTOSE-6P-atom8" elementType="O" x2="0.27966106" y2="-0.29378533"/> <atom id="FRUCTOSE-6P-atom9" elementType="O" x2="0.9971751" y2="-0.7485876"/> <atom id="FRUCTOSE-6P-atom10" elementType="P" x2="-0.70903957" y2="-0.3079096"/> <atom id="FRUCTOSE-6P-atom11" elementType="C" x2="0.67231643" y2="-0.519774"/> <atom id="FRUCTOSE-6P-atom12" elementType="H" x2="0.52259886" y2="-1.0"/> <atom id="FRUCTOSE-6P-atom13" elementType="O" x2="-0.70903957" y2="-0.60169494"/> <atom id="FRUCTOSE-6P-atom14" elementType="C" x2="0.52259886" y2="-0.8248588"/> <atom id="FRUCTOSE-6P-atom15" elementType="O" x2="-1.0" y2="-0.3079096"/> <atom id="FRUCTOSE-6P-atom16" elementType="O" x2="-0.70903957" y2="-0.005649686"/> <atom id="FRUCTOSE-6P-atom17" elementType="C" x2="0.67231643" y2="-0.7485876"/> <atom id="FRUCTOSE-6P-atom18" elementType="C" x2="0.028248549" y2="-0.8248588"/> <atom id="FRUCTOSE-6P-atom19" elementType="O" x2="0.52259886" y2="-0.65254235"/> </atomArray> <bondArray> <bond id="FRUCTOSE-6P-bond1" atomRefs="FRUCTOSE-6P-atom19 FRUCTOSE-6P-atom14" order="1"/> <bond id="FRUCTOSE-6P-bond2" atomRefs="FRUCTOSE-6P-atom18 FRUCTOSE-6P-atom14" order="1"/> <bond id="FRUCTOSE-6P-bond3" atomRefs="FRUCTOSE-6P-atom17 FRUCTOSE-6P-atom11" order="1"/> <bond id="FRUCTOSE-6P-bond4" atomRefs="FRUCTOSE-6P-atom15 FRUCTOSE-6P-atom10" order="1"/> <bond id="FRUCTOSE-6P-bond5" atomRefs="FRUCTOSE-6P-atom13 FRUCTOSE-6P-atom10" order="1"/> <bond id="FRUCTOSE-6P-bond6" atomRefs="FRUCTOSE-6P-atom12 FRUCTOSE-6P-atom14" order="1"/> <bond id="FRUCTOSE-6P-bond7" atomRefs="FRUCTOSE-6P-atom11 FRUCTOSE-6P-atom14" order="1"/> <bond id="FRUCTOSE-6P-bond8" atomRefs="FRUCTOSE-6P-atom10 FRUCTOSE-6P-atom16" order="2"/> <bond id="FRUCTOSE-6P-bond9" atomRefs="FRUCTOSE-6P-atom10 FRUCTOSE-6P-atom1" order="1"/> <bond id="FRUCTOSE-6P-bond10" atomRefs="FRUCTOSE-6P-atom9 FRUCTOSE-6P-atom17" order="1"/> <bond id="FRUCTOSE-6P-bond11" atomRefs="FRUCTOSE-6P-atom8 FRUCTOSE-6P-atom11" order="1"/> <bond id="FRUCTOSE-6P-bond12" atomRefs="FRUCTOSE-6P-atom7 FRUCTOSE-6P-atom18" order="1"/> <bond id="FRUCTOSE-6P-bond13" atomRefs="FRUCTOSE-6P-atom6 FRUCTOSE-6P-atom11" order="1"/> <bond id="FRUCTOSE-6P-bond14" atomRefs="FRUCTOSE-6P-atom5 FRUCTOSE-6P-atom4" order="1"/> <bond id="FRUCTOSE-6P-bond15" atomRefs="FRUCTOSE-6P-atom4 FRUCTOSE-6P-atom18" order="1"/> <bond id="FRUCTOSE-6P-bond16" atomRefs="FRUCTOSE-6P-atom4 FRUCTOSE-6P-atom8" order="1"/> <bond id="FRUCTOSE-6P-bond17" atomRefs="FRUCTOSE-6P-atom3 FRUCTOSE-6P-atom18" order="1"/> <bond id="FRUCTOSE-6P-bond18" atomRefs="FRUCTOSE-6P-atom2 FRUCTOSE-6P-atom4" order="1"/> <bond id="FRUCTOSE-6P-bond19" atomRefs="FRUCTOSE-6P-atom1 FRUCTOSE-6P-atom2" order="1"/> </bondArray> <formula concise="C 6 H 13 O 9 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">260.137</float> <string title="smiles">C(OP(O)(O)=O)[CH]1([CH](O)[CH](O)C(O)(O1)CO)</string> </molecule> </cml> CML D-fructose-6-P CAS 643-13-0 D-fructose-6-phosphate fructose-6-P fructose-6-phosphate fruc6p fru-6-P A-D-fructose-6-P fructose-6P H+ 1.0080000162124634 hydrogen ion H proton <cml> <molecule id="PROTON" title="H+" dictRef="dictPROTON"> <atomArray> <atom id="PROTON-atom1" elementType="H" x2="-1.0" y2="-1.0" formalCharge="1"/> </atomArray> <bondArray> </bondArray> <formula concise="H 1" formalCharge="1"/> <float title="molecularWeight" units="g/mol">1.008</float> <string title="smiles">[H+1]</string> </molecule> </cml> CML 1 fructose-1,6-bisphosphate 340.11700439453125 CAS 488-69-7 D-fructose-1,6-bisphosphate D-fructose-1,6-diphosphate &alpha;-D-fructose-1,6-diphosphate CML <cml> <molecule id="FRUCTOSE-16-DIPHOSPHATE" title="fructose-1,6-bisphosphate" dictRef="dictFRUCTOSE-16-DIPHOSPHATE"> <atomArray> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom1" elementType="H" x2="0.16364" y2="-0.97355"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom2" elementType="C" x2="0.28595" y2="-0.7686"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom3" elementType="C" x2="-0.34876" y2="-0.42149"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom4" elementType="H" x2="-0.34876" y2="-0.72893"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom5" elementType="O" x2="0.76529" y2="-0.53719"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom6" elementType="C" x2="0.28595" y2="-0.59008"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom7" elementType="P" x2="0.76529" y2="-0.7686"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom8" elementType="C" x2="-0.34876" y2="-0.59008"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom9" elementType="C" x2="0.16364" y2="-0.83471"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom10" elementType="O" x2="0.5405" y2="-0.7686"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom11" elementType="O" x2="0.28595" y2="-0.35868"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom12" elementType="O" x2="0.99669" y2="-0.7686"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom13" elementType="P" x2="-0.7686" y2="-0.42149"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom14" elementType="H" x2="-0.22645" y2="-0.69587"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom15" elementType="O" x2="-1.0" y2="-0.42149"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom16" elementType="O" x2="-0.0281" y2="-0.41157"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom17" elementType="O" x2="-0.7686" y2="-0.2"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom18" elementType="O" x2="-0.53388" y2="-0.42149"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom19" elementType="C" x2="-0.22645" y2="-0.83471"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom20" elementType="O" x2="0.76529" y2="-1.0"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom21" elementType="O" x2="-0.7686" y2="-0.66281"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom22" elementType="O" x2="0.16364" y2="-0.69587"/> <atom id="FRUCTOSE-16-DIPHOSPHATE-atom23" elementType="O" x2="-0.22645" y2="-0.97355"/> </atomArray> <bondArray> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond1" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom23 FRUCTOSE-16-DIPHOSPHATE-atom19" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond2" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom22 FRUCTOSE-16-DIPHOSPHATE-atom9" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond3" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom21 FRUCTOSE-16-DIPHOSPHATE-atom13" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond4" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom20 FRUCTOSE-16-DIPHOSPHATE-atom7" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond5" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom19 FRUCTOSE-16-DIPHOSPHATE-atom9" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond6" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom18 FRUCTOSE-16-DIPHOSPHATE-atom3" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond7" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom17 FRUCTOSE-16-DIPHOSPHATE-atom13" order="2"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond8" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom16 FRUCTOSE-16-DIPHOSPHATE-atom6" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond9" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom15 FRUCTOSE-16-DIPHOSPHATE-atom13" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond10" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom14 FRUCTOSE-16-DIPHOSPHATE-atom19" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond11" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom13 FRUCTOSE-16-DIPHOSPHATE-atom18" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond12" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom12 FRUCTOSE-16-DIPHOSPHATE-atom7" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond13" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom11 FRUCTOSE-16-DIPHOSPHATE-atom6" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond14" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom10 FRUCTOSE-16-DIPHOSPHATE-atom2" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond15" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom8 FRUCTOSE-16-DIPHOSPHATE-atom19" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond16" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom8 FRUCTOSE-16-DIPHOSPHATE-atom16" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond17" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom7 FRUCTOSE-16-DIPHOSPHATE-atom10" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond18" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom6 FRUCTOSE-16-DIPHOSPHATE-atom9" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond19" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom5 FRUCTOSE-16-DIPHOSPHATE-atom7" order="2"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond20" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom4 FRUCTOSE-16-DIPHOSPHATE-atom8" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond21" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom3 FRUCTOSE-16-DIPHOSPHATE-atom8" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond22" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom2 FRUCTOSE-16-DIPHOSPHATE-atom6" order="1"/> <bond id="FRUCTOSE-16-DIPHOSPHATE-bond23" atomRefs="FRUCTOSE-16-DIPHOSPHATE-atom1 FRUCTOSE-16-DIPHOSPHATE-atom9" order="1"/> </bondArray> <formula concise="C 6 H 14 O 12 P 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">340.117</float> <string title="smiles">C(OP(O)(O)=O)C1(O)(O[CH]([CH](O)[CH](O)1)COP(=O)(O)O)</string> <string title="systematicName">D-Fructose 1,6-bis(dihydrogenphosphate)</string> </molecule> </cml> fructose-1,6-diphosphate 1 1 <cml> <molecule id="ATP" title="ATP" dictRef="dictATP"> <atomArray> <atom id="ATP-atom1" elementType="C" x2="0.9971347" y2="-0.16905439"/> <atom id="ATP-atom2" elementType="P" x2="-0.4641834" y2="-0.68767905"/> <atom id="ATP-atom3" elementType="O" x2="-1.0" y2="-0.68767905"/> <atom id="ATP-atom4" elementType="N" x2="0.8767909" y2="-0.022922575"/> <atom id="ATP-atom5" elementType="O" x2="-0.12320912" y2="-0.5071633"/> <atom id="ATP-atom6" elementType="H" x2="0.5616046" y2="-0.8538682"/> <atom id="ATP-atom7" elementType="H" x2="0.6418339" y2="-0.7851003"/> <atom id="ATP-atom8" elementType="O" x2="-0.12320912" y2="-0.8653295"/> <atom id="ATP-atom9" elementType="O" x2="-0.4641834" y2="-0.8653295"/> <atom id="ATP-atom10" elementType="C" x2="0.5616046" y2="-0.7449857"/> <atom id="ATP-atom11" elementType="N" x2="0.8939829" y2="-0.3409742"/> <atom id="ATP-atom12" elementType="C" x2="0.6418339" y2="-0.89111745"/> <atom id="ATP-atom13" elementType="O" x2="-0.4641834" y2="-0.5071633"/> <atom id="ATP-atom14" elementType="C" x2="0.8939829" y2="-0.739255"/> <atom id="ATP-atom15" elementType="C" x2="0.82234967" y2="-0.89111745"/> <atom id="ATP-atom16" elementType="N" x2="0.4068768" y2="-0.10315186"/> <atom id="ATP-atom17" elementType="C" x2="0.4068768" y2="-0.29226357"/> <atom id="ATP-atom18" elementType="N" x2="0.5587393" y2="-0.3925501"/> <atom id="ATP-atom19" elementType="N" x2="0.5587393" y2="0.17478514"/> <atom id="ATP-atom20" elementType="O" x2="0.82234967" y2="-1.0"/> <atom id="ATP-atom21" elementType="C" x2="0.72206306" y2="-0.10315186"/> <atom id="ATP-atom22" elementType="C" x2="0.72206306" y2="-0.29226357"/> <atom id="ATP-atom23" elementType="C" x2="0.5587393" y2="-0.0028653145"/> <atom id="ATP-atom24" elementType="O" x2="0.6418339" y2="-1.0"/> <atom id="ATP-atom25" elementType="P" x2="-0.12320912" y2="-0.68767905"/> <atom id="ATP-atom26" elementType="H" x2="0.82234967" y2="-0.7851003"/> <atom id="ATP-atom27" elementType="O" x2="-0.81948423" y2="-0.8653295"/> <atom id="ATP-atom28" elementType="H" x2="0.8939829" y2="-0.8481375"/> <atom id="ATP-atom29" elementType="C" x2="0.36389685" y2="-0.68767905"/> <atom id="ATP-atom30" elementType="O" x2="0.7306591" y2="-0.66762173"/> <atom id="ATP-atom31" elementType="O" x2="-0.29226357" y2="-0.68767905"/> <atom id="ATP-atom32" elementType="O" x2="-0.81948423" y2="-0.5071633"/> <atom id="ATP-atom33" elementType="O" x2="0.05157602" y2="-0.68767905"/> <atom id="ATP-atom34" elementType="P" x2="-0.81948423" y2="-0.68767905"/> <atom id="ATP-atom35" elementType="O" x2="-0.63610315" y2="-0.68767905"/> </atomArray> <bondArray> <bond id="ATP-bond1" atomRefs="ATP-atom35 ATP-atom2" order="1"/> <bond id="ATP-bond2" atomRefs="ATP-atom34 ATP-atom35" order="1"/> <bond id="ATP-bond3" atomRefs="ATP-atom33 ATP-atom29" order="1"/> <bond id="ATP-bond4" atomRefs="ATP-atom32 ATP-atom34" order="2"/> <bond id="ATP-bond5" atomRefs="ATP-atom31 ATP-atom25" order="1"/> <bond id="ATP-bond6" atomRefs="ATP-atom30 ATP-atom14" order="1"/> <bond id="ATP-bond7" atomRefs="ATP-atom29 ATP-atom10" order="1"/> <bond id="ATP-bond8" atomRefs="ATP-atom28 ATP-atom14" order="1"/> <bond id="ATP-bond9" atomRefs="ATP-atom27 ATP-atom34" order="1"/> <bond id="ATP-bond10" atomRefs="ATP-atom26 ATP-atom15" order="1"/> <bond id="ATP-bond11" atomRefs="ATP-atom25 ATP-atom33" order="1"/> <bond id="ATP-bond12" atomRefs="ATP-atom24 ATP-atom12" order="1"/> <bond id="ATP-bond13" atomRefs="ATP-atom23 ATP-atom16" order="A"/> <bond id="ATP-bond14" atomRefs="ATP-atom22 ATP-atom21" order="A"/> <bond id="ATP-bond15" atomRefs="ATP-atom21 ATP-atom4" order="A"/> <bond id="ATP-bond16" atomRefs="ATP-atom21 ATP-atom23" order="A"/> <bond id="ATP-bond17" atomRefs="ATP-atom20 ATP-atom15" order="1"/> <bond id="ATP-bond18" atomRefs="ATP-atom19 ATP-atom23" order="1"/> <bond id="ATP-bond19" atomRefs="ATP-atom18 ATP-atom22" order="A"/> <bond id="ATP-bond20" atomRefs="ATP-atom17 ATP-atom18" order="A"/> <bond id="ATP-bond21" atomRefs="ATP-atom16 ATP-atom17" order="A"/> <bond id="ATP-bond22" atomRefs="ATP-atom14 ATP-atom15" order="1"/> <bond id="ATP-bond23" atomRefs="ATP-atom14 ATP-atom11" order="1"/> <bond id="ATP-bond24" atomRefs="ATP-atom13 ATP-atom2" order="2"/> <bond id="ATP-bond25" atomRefs="ATP-atom12 ATP-atom15" order="1"/> <bond id="ATP-bond26" atomRefs="ATP-atom11 ATP-atom22" order="A"/> <bond id="ATP-bond27" atomRefs="ATP-atom10 ATP-atom12" order="1"/> <bond id="ATP-bond28" atomRefs="ATP-atom10 ATP-atom30" order="1"/> <bond id="ATP-bond29" atomRefs="ATP-atom9 ATP-atom2" order="1"/> <bond id="ATP-bond30" atomRefs="ATP-atom8 ATP-atom25" order="1"/> <bond id="ATP-bond31" atomRefs="ATP-atom7 ATP-atom12" order="1"/> <bond id="ATP-bond32" atomRefs="ATP-atom6 ATP-atom10" order="1"/> <bond id="ATP-bond33" atomRefs="ATP-atom5 ATP-atom25" order="2"/> <bond id="ATP-bond34" atomRefs="ATP-atom4 ATP-atom1" order="A"/> <bond id="ATP-bond35" atomRefs="ATP-atom3 ATP-atom34" order="1"/> <bond id="ATP-bond36" atomRefs="ATP-atom2 ATP-atom31" order="1"/> <bond id="ATP-bond37" atomRefs="ATP-atom1 ATP-atom11" order="A"/> </bondArray> <formula concise="C 10 H 16 N 5 O 13 P 3" formalCharge="-4"/> <float title="molecularWeight" units="g/mol">507.183</float> <string title="smiles">[CH]3(n1(c2(c(nc1)c(N)ncn2)))(O[CH]([CH](O)[CH](O)3)COP(=O)(O)OP(O)(=O)OP(O)(=O)O)</string> </molecule> </cml> CML 56-65-5 CAS adenosine-5'-triphosphate adenylpyrophosphate adenosine-triphosphate ATP 507.1830139160156 6PFRUCTPHOS-RXN -3.4 This enzyme is an isozyme with phosphofructokinase-2. The nucleotide sequences of the genes are not similar |CITS: [85203917]|. The tetrameric species is the only one which can bind both substrates and effectors, and thus have both catalytic and regulatory properties. The C terminal end of the peptide is required for allosteric properties.|CITS: [90276415]| Crystal structures have been solved with and without activators and inhibitors. |CITS: [89342465], [89125622]| cellular_component unknown GO GO:0008372 MIKKIGVLTSGGDAPGMNAAIRGVVRSALTEGLEVMGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFRDENIRAVAIENLKKRGIDALVVIGGDGSYMGAMRLTEMGFPCIGLPGTIDNDIKGTDYTIGFFTALSTVVEAIDRLRDTSSSHQRISVVEVMGRYCGDLTLAAAIAGGCEFVVVPEVEFSREDLVNEIKAGIAKGKKHAIVAITEHMCDVDELAHFIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIDLLLAGYGGRCVGIQNEQLVHHDIIDAIENMKRPFKGDWLDCAKKLY Escherichia coli K-12 83333 taxon Escherichia coli K-12 P06998 SWISS-PROT Ortholog EcoO157Cyc PFKA-MONOMER PDB 2PFK NP_418351 RefSeq 6-phosphofructokinase-1 monomer b3916 PIR PfkA SWISS-MODEL P06998 B3916 4 6PFK-1-CPX fructose-6-p-1-kinase fructose-6-phosphate-1-phosphotransferase REVERSIBLE ACTIVATION-NONALLOSTERIC 1,3-diphosphoglycerate 13-dpg CAS 1981-49-3 CML <cml> <molecule id="DPG" title="3-phospho-D-glyceroyl-phosphate" dictRef="dictDPG"> <atomArray> <atom id="DPG-atom1" elementType="C" x2="-0.02174" y2="-0.73602"/> <atom id="DPG-atom2" elementType="P" x2="0.73292" y2="-0.48137"/> <atom id="DPG-atom3" elementType="O" x2="0.73292" y2="-0.21739"/> <atom id="DPG-atom4" elementType="P" x2="-0.73602" y2="-0.48137"/> <atom id="DPG-atom5" elementType="O" x2="0.49379" y2="-0.48137"/> <atom id="DPG-atom6" elementType="O" x2="-0.73602" y2="-0.21739"/> <atom id="DPG-atom7" elementType="O" x2="-0.52484" y2="-0.48137"/> <atom id="DPG-atom8" elementType="O" x2="-0.02174" y2="-1.0"/> <atom id="DPG-atom9" elementType="C" x2="-0.25776" y2="-0.48137"/> <atom id="DPG-atom10" elementType="O" x2="0.99689" y2="-0.48137"/> <atom id="DPG-atom11" elementType="O" x2="-0.25776" y2="-0.21739"/> <atom id="DPG-atom12" elementType="O" x2="-0.73602" y2="-0.74534"/> <atom id="DPG-atom13" elementType="O" x2="0.73292" y2="-0.74534"/> <atom id="DPG-atom14" elementType="O" x2="-1.0" y2="-0.48137"/> <atom id="DPG-atom15" elementType="C" x2="0.21739" y2="-0.48137"/> </atomArray> <bondArray> <bond id="DPG-bond1" atomRefs="DPG-atom15 DPG-atom5" order="1"/> <bond id="DPG-bond2" atomRefs="DPG-atom9 DPG-atom1" order="1"/> <bond id="DPG-bond3" atomRefs="DPG-atom9 DPG-atom11" order="2"/> <bond id="DPG-bond4" atomRefs="DPG-atom7 DPG-atom9" order="1"/> <bond id="DPG-bond5" atomRefs="DPG-atom5 DPG-atom2" order="1"/> <bond id="DPG-bond6" atomRefs="DPG-atom4 DPG-atom7" order="1"/> <bond id="DPG-bond7" atomRefs="DPG-atom4 DPG-atom6" order="1"/> <bond id="DPG-bond8" atomRefs="DPG-atom4 DPG-atom12" order="1"/> <bond id="DPG-bond9" atomRefs="DPG-atom4 DPG-atom14" order="2"/> <bond id="DPG-bond10" atomRefs="DPG-atom2 DPG-atom3" order="1"/> <bond id="DPG-bond11" atomRefs="DPG-atom2 DPG-atom13" order="1"/> <bond id="DPG-bond12" atomRefs="DPG-atom2 DPG-atom10" order="2"/> <bond id="DPG-bond13" atomRefs="DPG-atom1 DPG-atom15" order="1"/> <bond id="DPG-bond14" atomRefs="DPG-atom1 DPG-atom8" order="1"/> </bondArray> <formula concise="C 3 H 8 O 10 P 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">266.038</float> <string title="smiles">C(OP(O)(O)=O)(=O)C(O)COP(O)(O)=O</string> </molecule> </cml> 266.0379943847656 1,3-bis-phosphoglycerate 3-phosphoglyceroyl-P phosphoglyceroyl-P 3-phosphoglyceroyl-phosphate dpg 1,3-biphosphoglycerate 3-P-glyceroyl-P 3-phospho-D-glyceroyl-phosphate 1,3-diphosphateglycerate glycerate 1,3-biphosphate glycerate 1,3-diphosphate P-glyceroyl-P 186.05799865722656 g3p 3-phospho-glyceric acid 3-pg 3-phospho-(R)-glycerate 3-phosphoglycerate glycerate 3-phosphate glycerate-3-P D-Glycerate 3-phosphate 3-P-D-glycerate 820-11-1 CAS 3-phospho-D-glycerate 3-P-glycerate <cml> <molecule id="G3P" title="3-phosphoglycerate" dictRef="dictG3P"> <atomArray> <atom id="G3P-atom1" elementType="C" x2="5.7" y2="-0.5"/> <atom id="G3P-atom2" elementType="C" x2="5.7" y2="-1.25"/> <atom id="G3P-atom3" elementType="C" x2="5.6995" y2="0.25"/> <atom id="G3P-atom4" elementType="O" x2="6.3499" y2="0.6232"/> <atom id="G3P-atom5" elementType="O" x2="5.0484" y2="0.6225"/> <atom id="G3P-atom6" elementType="O" x2="6.45" y2="-0.4998"/> <atom id="G3P-atom7" elementType="P" x2="7.0977" y2="-1.6376"/> <atom id="G3P-atom8" elementType="O" x2="7.0887" y2="-2.3709"/> <atom id="G3P-atom9" elementType="O" x2="7.8767" y2="-1.6513"/> <atom id="G3P-atom10" elementType="O" x2="7.1108" y2="-0.9002"/> <atom id="G3P-atom11" elementType="O" x2="6.3477" y2="-1.6285"/> </atomArray> <bondArray> <bond id="G3P-bond1" atomRefs="G3P-atom7 G3P-atom11" order="1"/> <bond id="G3P-bond2" atomRefs="G3P-atom7 G3P-atom10" order="1"/> <bond id="G3P-bond3" atomRefs="G3P-atom7 G3P-atom9" order="2"/> <bond id="G3P-bond4" atomRefs="G3P-atom7 G3P-atom8" order="1"/> <bond id="G3P-bond5" atomRefs="G3P-atom2 G3P-atom11" order="1"/> <bond id="G3P-bond6" atomRefs="G3P-atom1 G3P-atom6" order="1"/> <bond id="G3P-bond7" atomRefs="G3P-atom1 G3P-atom3" order="1"/> <bond id="G3P-bond8" atomRefs="G3P-atom3 G3P-atom5" order="2"/> <bond id="G3P-bond9" atomRefs="G3P-atom3 G3P-atom4" order="1"/> <bond id="G3P-bond10" atomRefs="G3P-atom1 G3P-atom2" order="1"/> </bondArray> <formula concise="C 3 H 7 O 7 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">186.058</float> <string title="smiles">C(OP(=O)(O)O)C(O)C(=O)O</string> </molecule> </cml> CML 1 PGAM PHOSPHOGLYCERATE PHOSPHOMUTASE 5.4.2.1 1.1 PHOSPHOGLYCEROMUTASE 3PGAREARR-RXN 1 CML <cml> <molecule id="2-PG" title="2-phosphoglycerate" dictRef="dict2-PG"> <atomArray> <atom id="2-PG-atom1" elementType="C" x2="2.8208" y2="-1.4"/> <atom id="2-PG-atom2" elementType="C" x2="2.8208" y2="-0.65"/> <atom id="2-PG-atom3" elementType="O" x2="2.1713" y2="-1.775"/> <atom id="2-PG-atom4" elementType="O" x2="3.4704" y2="-1.775"/> <atom id="2-PG-atom5" elementType="C" x2="2.8208" y2="0.1"/> <atom id="2-PG-atom6" elementType="O" x2="3.4704" y2="0.475"/> <atom id="2-PG-atom7" elementType="P" x2="1.2603" y2="-0.6662"/> <atom id="2-PG-atom8" elementType="O" x2="1.2502" y2="0.0671"/> <atom id="2-PG-atom9" elementType="O" x2="0.452" y2="-0.652"/> <atom id="2-PG-atom10" elementType="O" x2="1.2663" y2="-1.4037"/> <atom id="2-PG-atom11" elementType="O" x2="2.0727" y2="-0.6505"/> </atomArray> <bondArray> <bond id="2-PG-bond1" atomRefs="2-PG-atom7 2-PG-atom11" order="1"/> <bond id="2-PG-bond2" atomRefs="2-PG-atom7 2-PG-atom10" order="1"/> <bond id="2-PG-bond3" atomRefs="2-PG-atom7 2-PG-atom9" order="2"/> <bond id="2-PG-bond4" atomRefs="2-PG-atom7 2-PG-atom8" order="1"/> <bond id="2-PG-bond5" atomRefs="2-PG-atom5 2-PG-atom6" order="1"/> <bond id="2-PG-bond6" atomRefs="2-PG-atom2 2-PG-atom5" order="1"/> <bond id="2-PG-bond7" atomRefs="2-PG-atom2 2-PG-atom11" order="1"/> <bond id="2-PG-bond8" atomRefs="2-PG-atom1 2-PG-atom4" order="2"/> <bond id="2-PG-bond9" atomRefs="2-PG-atom1 2-PG-atom3" order="1"/> <bond id="2-PG-bond10" atomRefs="2-PG-atom1 2-PG-atom2" order="1"/> </bondArray> <formula concise="C 3 H 7 O 7 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">186.058</float> <string title="smiles">C(O)(=O)C(CO)OP(=O)(O)O</string> </molecule> </cml> glycerate 2-phosphate 2-phospho-D-glycerate CAS 2553-59-5 2-P-D-glycerate 2-phosphoglyceric acid 2-P-glycerate D-Glycerate 2-phosphate 186.05799865722656 2-pg 2-phosphoglycerate D-phosphoglycerate 2,3-phosphomutase PGAM, cofactor independent REVERSIBLE phosphoglycerate mutase, BPG-independent Ortholog EcoO157Cyc YIBO-MONOMER PgmI MLVSKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVIRAEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAVEGGKLSDIAPTMLSLMGMEIPQEMTGKPLFIVE P37689 SWISS-PROT B3612 GpmC PIR b3612 GpmM NP_418069 RefSeq PGMI-MONOMER YibO GpmI phosphoglycerate mutase, cofactor independent Mn<SUP>++</SUP> Mn<SUP>+2</SUP> Mn2+ manganese ion 1.0 iPGM BPG-independent PGAM E. coli contains three phosphoglycerate mutases. Two are 2,3-bisphosphoglycerate-dependent enzymes, encoded by the gpmA and gpmB genes. The third is a 2,3-bisphosphoglycerate-independent enzyme encoded by the pgmI gene. The two cofactor-dependent enzymes are similar in sequence while the cofactor-independent enzyme is unrelated. The cofactor-dependent enzymes have ten times higher specific activity compared to the cofactor-independent enzyme. |CITS: [99364512]| phosphoglyceromutase phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent phosphoglycerate phosphomutase D-phosphoglycerate 2,3-phosphomutase 1 E. coli contains three phosphoglycerate mutases. Two are 2,3-bisphosphoglyerate-dependent enzymes, encoded by the gpmA and gpmB genes. The third is a 2,3-bisphosphoglyerate-independent enzyme encoded by the pgmI gene. |CITS: [99364512]| PHOSGLYCMUTASE 2 GpmA GpmA Regulation has been described |CITS: [11101675]|. Transcription is regulated by Fur |CITS: [11101675]|. SWISS-PROT P31217 Pgm SWISS-MODEL P31217 PgmA Gpm B0755 b0755 PIR NP_415276 RefSeq MAVTKLVLVRHGESQWNKENRFTGWYDVDLSEKGVSEAKAAGKLLKEEGYSFDFAYTSVLKRAIHTLWNVLDELDQAWLPVEKSWKLNERHYGALQGLNKAETAEKYGDEQVKQWRRGFAVTPPELTKDDERYPGHDPRYAKLSEKELPLTESLALTIDRVIPYWNETILPRMKSGERVIIAAHGNSLRALVKYLDNMSEEEILELNIPTGVPLVYEFDENFKPLKRYYLGNADEIAAKAAAVANQGKAK PGAM 1 phosphoglycerate mutase 1 phosphoglyceromutase 1 BPG-dependent PGAM1 REVERSIBLE phosphoglycerate phosphomutase 1 REVERSIBLE 2,3-diphospho-D-glycerate 2-phospho-D-glycerate hydrolyase phosphopyruvate hydratase enolase 1 P-enol-pyr P-enol-pyruvate PEP c00074 LIGAND <cml> <molecule id="PHOSPHO-ENOL-PYRUVATE" title="phosphoenolpyruvate" dictRef="dictPHOSPHO-ENOL-PYRUVATE"> <atomArray> <atom id="PHOSPHO-ENOL-PYRUVATE-atom1" elementType="O" x2="-0.57576" y2="-0.15789"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom2" elementType="O" x2="0.24721" y2="0.33652"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom3" elementType="O" x2="-1.0" y2="-0.57576"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom4" elementType="C" x2="-0.57576" y2="0.26635"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom5" elementType="C" x2="-0.9075" y2="0.52791"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom6" elementType="O" x2="-0.15152" y2="-0.57576"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom7" elementType="O" x2="-0.57576" y2="-1.0"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom8" elementType="O" x2="-0.10686" y2="0.99681"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom9" elementType="P" x2="-0.57576" y2="-0.57576"/> <atom id="PHOSPHO-ENOL-PYRUVATE-atom10" elementType="C" x2="-0.10686" y2="0.57257"/> </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 5 O 6 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">168.043</float> <string title="smiles">C=C(C(=O)O)OP(O)(=O)O</string> </molecule> </cml> CML phosphoenolpyruvate 73-89-2 CAS 168.04299926757812 ENOLASE 2-PHOSPHOGLYCERATE DEHYDRATASE hydrogen oxide water H2O H20 18.014999389648438 7732-18-5 CAS CML <cml> <molecule id="WATER" title="H2O" dictRef="dictWATER"> <atomArray> <atom id="WATER-atom1" elementType="O" x2="0.08287" y2="-0.19337"/> <atom id="WATER-atom2" elementType="H" x2="-1.0" y2="-0.74586"/> <atom id="WATER-atom3" elementType="H" x2="0.99448" y2="-1.0"/> </atomArray> <bondArray> <bond id="WATER-bond1" atomRefs="WATER-atom3 WATER-atom1" order="1"/> <bond id="WATER-bond2" atomRefs="WATER-atom2 WATER-atom1" order="1"/> </bondArray> <formula concise="H 2 O 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">18.015</float> <string title="smiles">[OH2]</string> </molecule> </cml> 1 2-phosphoglycerate dehydration 0.4 4.2.1.11 There are two active sites per active dimer. Functionally there are many similarities between E. coli enolase and other enolases studied. Thus the dependence on Mg for activity and the inhibition by fluoride in the presence of phosphate are quantitatively very similar for all enolases. Other catalytic parameters are also similar but minor quantitative distinctions indicate that E. coli enolase is more closely related to yeast enolase than to enolases from vertebrate muscle. The pH optimum of 8.1 is significantly higher than that for vertebrate enolases and even somewhat above that of yeast and plant enolases. |CITS:[72060411]| Wold F 1971 Spring TG J Biol Chem 1971;246(22);6797-802 4942326 PubMed The purification and characterization of Escherichia coli enolase. 2-phosphoglycerate dehydratase 2-phospho-D glycerate phosphotransferase The enzyme denatures in the absence of Mg. When E. coli enolase was treated with EDTA in attempts to remove all residual activity prior to the Mg activation studies, it was found that the enzyme was unstable in the absence of Mg and that substantial and irreversible loss of activity was observed after very short exposure of the enzyme to EDTA. |CITS:[72060411]| 2 MSKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALELRDGDKSRFLGKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGTENKSKFGANAILAVSLANAKAAAAAKGMPLYEHIAELNGTPGKYSMPVPMMNIINGGEHADNNVDIQEFMIQPVGAKTVKEAIRMGSEVFHHLAKVLKAKGMNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASEFYKDGKYVLAGEGNKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDGFAYQTKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTETLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVAKYNQLIRIEEALGEKAPYNGRKEIKGQA SWISS-PROT P08324 P08324 SWISS-MODEL Eno PIR b2779 ENO-MONOMER EcoO157Cyc Ortholog B2779 Eno NP_417259 RefSeq ENOLASE-CPLX INHIBITION-UNKMECH F fluoride ion fluoride F- 1.0 high concentrations of Mg+2 and ADP |CITS:[89228557]| INHIBITION-UNKMECH 39.097999572753906 K+ potassium ion <cml> <molecule id="K+" title="K+" dictRef="dictK+"> <atomArray> <atom id="K+-atom1" elementType="K" x2="-1.0" y2="-1.0" formalCharge="1"/> </atomArray> <bondArray> </bondArray> <formula concise="K 1" formalCharge="1"/> <float title="molecularWeight" units="g/mol">39.098</float> <string title="smiles">[K+1]</string> </molecule> </cml> CML 1.0 pyruvate kinase phosphoenol transphosphorylase phosphoenolpyruvate dephosphorylation pyruvate phosphorylation pyroracemic acid 2-oxo-propionic acid alpha-ketopropionic acid pyruvate 2-oxopropanoate 2-oxopropanoic acid BTS pyruvic acid CML <cml> <molecule id="PYRUVATE" title="pyruvate" dictRef="dictPYRUVATE"> <atomArray> <atom id="PYRUVATE-atom1" elementType="C" x2="0.36301" y2="-0.2363"/> <atom id="PYRUVATE-atom2" elementType="C" x2="-1.0" y2="-0.2774"/> <atom id="PYRUVATE-atom3" elementType="O" x2="-0.34247" y2="0.87329"/> <atom id="PYRUVATE-atom4" elementType="C" x2="-0.34247" y2="0.10959"/> <atom id="PYRUVATE-atom5" elementType="O" x2="0.36301" y2="-1.0"/> <atom id="PYRUVATE-atom6" elementType="O" x2="0.99658" y2="0.18836"/> </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 4 O 3" formalCharge="0"/> <float title="molecularWeight" units="g/mol">88.063</float> <string title="smiles">C(=O)(O)C(=O)C</string> </molecule> </cml> acetylformic acid UMBBD c0159 127-17-3 CAS 88.06300354003906 LIGAND c00022 1 2.7.1.40 pyruvate 2-0-phosphotransferase REVERSIBLE type I pyruvate kinase Pyruvate kinase I is strongly activated by fructose 1,6 bisphosphate and shows sigmoid kinetics with respect to the substrate phophoenolpyruvate. The dependences of the reaction rate on the concentrations of phosphoenolpyruvate, Mg<SUP>+2</SUP>, and Mn<SUP>+2</SUP> are sigmoid. These dependences become hyperbolic on addition of fructose 1,6 bisphosphate. The dependences of the reaction rate on the concentration of ADP are always hyperbolic. The catalytic active complex of E. coli pyruvate kinase is formed by only one conformational state of the enzyme, state R1. This state binds randomly the Mg<SUP>+2</SUP> free ligands ADP or phosphoenolpyruvate. Thereafter, the active enzyme complex is formed by binding Mg<SUP>+2</SUP>-PEP or Mg<SUP>+2</SUP>ADP respectively. State R2 of coli pyruvate kinase binds randomly ADP and Mg<SUP>+2</SUP>. It is the only state in which Mg<SUP>+2</SUP> can bind to the free enzyme. Mg<SUP>+2</SUP> is not necesary for the binding of ADP, PEP an ATP. Mg<SUP>+2</SUP> can inhibit either by binding to the state R2 or by lowering the concentration of Mg<SUP>+2</SUP>, free ADP and PEP through complex formation. ATP inhibits by virtue of three effects: increase in ionic strength, complex-formation with Mg<SUP>+2</SUP> when this metal ion acts as an activator and binding to the state R3. However when conditions are such that Mg<SUP>+2</SUP> is an inhibitor, then ATP is expected to activate because of complex formation with Mg<SUP>+2</SUP>. In general, one can say that the ligands Mg<SUP>+2</SUP> and ATP cannot be classified as inhibitors or activators because their regulatory effect on the reaction rate depends on the concentration of the other ligands.|CITS:[81159972]| By addition of fructose-1,6-bisphosphate the sigmoid kinetics with respect to phosphoenolpyruvate and Mg<SUP>+2</SUP> is abolished and the activity of the enzyme is described by classical saturation kinetics. This is explained by exclusive binding of fructose 1,6 bisphosphate at an allosteric site of the conformational state that forms the active complex. Ca<SUP>+2</SUP> is an activator of the enzyme at low Mg<SUP>+2</SUP> and Ca<SUP>+2</SUP> concentrations; otherwise it is an inhibitor. These effects can be understood by assuming that Ca<SUP>+2</SUP> has the same binding properties as Mg<SUP>+2</SUP>, although it does not allow a catalytic turnover.|CITS:[83282602]| The enzyme requires both bivalent and monovalent cations. |CITS: [90336973]| pyruvate kinase I pyruvate kinase F PKI-COMPLEX 4 PIR b1676 SWISS-PROT P14178 1E0T PDB B1676 NP_416191 RefSeq MKKTKIVCTIGPKTESEEMLAKMLDAGMNVMRLNFSHGDYAEHGQRIQNLRNVMSKTGKTAAILLDTKGPEIRTMKLEGGNDVSLKAGQTFTFTTDKSVIGNSEMVAVTYEGFTTDLSVGNTVLVDDGLIGMEVTAIEGNKVICKVLNNGDLGENKGVNLPGVSIALPALAEKDKQDLIFGCEQGVDFVAASFIRKRSDVIEIREHLKAHGGENIHIISKIENQEGLNNFDEILEASDGIMVARGDLGVEIPVEEVIFAQKMMIEKCIRARKVVITATQMLDSMIKNPRPTRAEAGDVANAILDGTDAVMLSGESAKGKYPLEAVSIMATICERTDRVMNSRLEFNNDNRKLRITEAVCRGAVETAEKLDAPLIVVATQGGKSARAVRKYFPDATILALTTNEKTAHQLVLSKGVVPQLVKEITSTDDFYRLGKELALQSGLAHKGDVVVMVSGALVPSGTTNTASVHVL Type I pyruvate kinase is made up of 522 amino acids. Neither type I nor II contains tryptophan. The two forms of the enzyme, I and II are different proteins.|CITS:[83114522]| Pyruvate kinase F was previously referred to as pyruvate kinase B, now as I |CITS:[84029179]| A free N-terminal amino acid can be detected in both forms of pyruvate kinase it corresponds to methionine for type I and serine for type II.|CITS:[83114522]| Comparison with the known primary structures shows that bacterial enzymes lack a substantial portion of the N-terminal sequence with respect to pyruvate kinases from vertebrates. |CITS:[91315755]| P14178 SWISS-MODEL pyruvate kinase I monomer 1E0U PDB PykF 1PKY PDB EcoO157Cyc Ortholog PYKF-MONOMER Pyruvate kinase I and pyruvate kinase II differ in physical and chemical properties as well as in their kinetic behavior. Although the two forms are under independent genetic control they do coexist in a wide range of nutritional and metabolic states. The two forms are not interconvertible. Both show positive cooperative effects with respect to the substrate phosphoenolpyruvate.|CITS:[83114522]| The enzyme has a low nucleotide specificity and the 5'-diphosphates of guanosine, inosine, uridine and cytidine can all serve as phospho acceptors.|CITS: [90336973]| Form I from E coli unlike form II is remarkably stable. |CITS:[91315755]| phosphoenolpyruvate kinase ACTIVATION-UNKMECH 1.0 40.08000183105469 <cml> <molecule id="CA+2" title="Ca2+" dictRef="dictCA+2"> <atomArray> <atom id="CA+2-atom1" elementType="CA" x2="-1.0" y2="-1.0" formalCharge="2"/> </atomArray> <bondArray> </bondArray> <formula concise="CA 1" formalCharge="2"/> <float title="molecularWeight" units="g/mol">40.08</float> <string title="smiles">[Ca+2]</string> </molecule> </cml> CML calcium ion Ca2+ Ca<SUP>++</SUP> Ca<SUP>+2</SUP> An activator only at low Mg<SUP>+2</SUP> and Ca<SUP>+2</SUP> concentrations, otherwise it is an inhibitor. |CITS: [83282602]| INHIBITION-UNKMECH high concentrations of Mg+2 and ADP |CITS:[89228557]| Pyruvate kinase II displays only limited cooperativity amoung phosphoenolpyruvate binding sites and is allosterically activated by AMP and several sugar phosphates |CITS:[91315755]| The enzyme requires both bivalent and monovalent cations. |CITS: [90336973]| type II pyruvate kinase pyruvate kinase II PYKA-MONOMER Ortholog EcoO157Cyc RefSeq NP_416368 pyruvate kinase II monomer P21599 SWISS-PROT MSRRLRRTKIVTTLGPATDRDNNLEKVIAAGANVVRMNFSHGSPEDHKMRADKVREIAAKLGRHVAILGDLQGPKIRVSTFKEGKVFLNIGDKFLLDANLGKGEGDKEKVGIDYKGLPADVVPGDILLLDDGRVQLKVLEVQGMKVFTEVTVGGPLSNNKGINKLGGGLSAEALTEKDKADIKTAALIGVDYLAVSFPRCGEDLNYARRLARDAGCDAKIVAKVERAEAVCSQDAMDDIILASDVVMVARGDLGVEIGDPELVGIQKALIRRARQLNRAVITATQMMESMITNPMPTRAEVMDVANAVLDGTDAVMLSAETAAGQYPSETVAAMARVCLGAEKIPSINVSKHRLDVQFDNVEEAIAMSAMYAANHLKGVTAIITMTESGRTALMTSRISSGLPIFAMSRHERTLNLTALYRGVTPVHFDSANDGVAAASEAVNLLRDKGYLMSGDLVIVTQGDVMSTVGSTNTTRILTVE b1854 PIR PykA P21599 SWISS-MODEL B1854 There are 2 genes, pykA and pykF, for 2 isozymes 4 PKII-CPLX REVERSIBLE pyruvate kinase A INHIBITION-UNKMECH high concentrations of Mg+2 and ADP |CITS:[89228557]| 1.0 succinyl-S-coenzyme-A succ-S-coenzyme-A suc-coa succ-CoA succ-coenzyme-A CML <cml> <molecule id="SUC-COA" title="succinyl-CoA" dictRef="dictSUC-COA"> <atomArray> <atom id="SUC-COA-atom1" elementType="C" x2="0.88294" y2="-0.23077"/> <atom id="SUC-COA-atom2" elementType="N" x2="-1.0" y2="-0.14381"/> <atom id="SUC-COA-atom3" elementType="C" x2="0.8194" y2="-0.35452"/> <atom id="SUC-COA-atom4" elementType="C" x2="-0.60535" y2="0.11371"/> <atom id="SUC-COA-atom5" elementType="N" x2="0.60535" y2="0.05017"/> <atom id="SUC-COA-atom6" elementType="O" x2="-0.86622" y2="0.11371"/> <atom id="SUC-COA-atom7" elementType="P" x2="0.8194" y2="-0.82274"/> <atom id="SUC-COA-atom8" elementType="C" x2="-0.86622" y2="-0.06355"/> <atom id="SUC-COA-atom9" elementType="O" x2="0.8194" y2="-0.46154"/> <atom id="SUC-COA-atom10" elementType="C" x2="0.98662" y2="0.21405"/> <atom id="SUC-COA-atom11" elementType="O" x2="0.8194" y2="-1.0"/> <atom id="SUC-COA-atom12" elementType="N" x2="0.45151" y2="0.29097"/> <atom id="SUC-COA-atom13" elementType="C" x2="0.22408" y2="-0.57525"/> <atom id="SUC-COA-atom14" elementType="O" x2="0.71572" y2="-0.14047"/> <atom id="SUC-COA-atom15" elementType="O" x2="-0.66221" y2="-0.41472"/> <atom id="SUC-COA-atom16" elementType="N" x2="-0.52843" y2="-0.6689"/> <atom id="SUC-COA-atom17" elementType="O" x2="-0.31773" y2="-0.04013"/> <atom id="SUC-COA-atom18" elementType="C" x2="0.08696" y2="-0.67559"/> <atom id="SUC-COA-atom19" elementType="O" x2="0.48829" y2="-0.39799"/> <atom id="SUC-COA-atom20" elementType="C" x2="0.48829" y2="-0.57525"/> <atom id="SUC-COA-atom21" elementType="O" x2="0.21405" y2="0.13712"/> <atom id="SUC-COA-atom22" elementType="C" x2="-0.66221" y2="-0.59197"/> <atom id="SUC-COA-atom23" elementType="H" x2="0.8194" y2="-0.24749"/> <atom id="SUC-COA-atom24" elementType="C" x2="0.58863" y2="0.37793"/> <atom id="SUC-COA-atom25" elementType="O" x2="0.21405" y2="-0.21739"/> <atom id="SUC-COA-atom26" elementType="C" x2="-0.60535" y2="-0.06355"/> <atom id="SUC-COA-atom27" elementType="N" x2="0.88294" y2="0.05686"/> <atom id="SUC-COA-atom28" elementType="C" x2="-0.60535" y2="-0.2408"/> <atom id="SUC-COA-atom29" elementType="O" x2="0.8194" y2="-0.62542"/> <atom id="SUC-COA-atom30" elementType="O" x2="-0.11371" y2="0.13712"/> <atom id="SUC-COA-atom31" elementType="H" x2="0.61873" y2="-0.24749"/> <atom id="SUC-COA-atom32" elementType="C" x2="-0.47492" y2="-0.14381"/> <atom id="SUC-COA-atom33" elementType="O" x2="0.04013" y2="-0.04013"/> <atom id="SUC-COA-atom34" elementType="O" x2="-0.11371" y2="-0.21739"/> <atom id="SUC-COA-atom35" elementType="O" x2="0.99666" y2="-0.82274"/> <atom id="SUC-COA-atom36" elementType="S" x2="-0.06355" y2="-0.56522"/> <atom id="SUC-COA-atom37" elementType="C" x2="-0.20401" y2="-0.6689"/> <atom id="SUC-COA-atom38" elementType="O" x2="0.64548" y2="-0.65552"/> <atom id="SUC-COA-atom39" elementType="C" x2="0.7291" y2="0.29766"/> <atom id="SUC-COA-atom40" elementType="C" x2="-0.35452" y2="-0.57525"/> <atom id="SUC-COA-atom41" elementType="O" x2="0.08696" y2="-0.85284"/> <atom id="SUC-COA-atom42" elementType="C" x2="0.35786" y2="-0.66555"/> <atom id="SUC-COA-atom43" elementType="O" x2="0.38462" y2="-0.04013"/> <atom id="SUC-COA-atom44" elementType="C" x2="-0.86957" y2="-0.67559"/> <atom id="SUC-COA-atom45" elementType="N" x2="0.87291" y2="0.3612"/> <atom id="SUC-COA-atom46" elementType="H" x2="0.55184" y2="-0.33779"/> <atom id="SUC-COA-atom47" elementType="P" x2="0.21405" y2="-0.04013"/> <atom id="SUC-COA-atom48" elementType="C" x2="0.7291" y2="0.14047"/> <atom id="SUC-COA-atom49" elementType="O" x2="-0.74916" y2="-0.32107"/> <atom id="SUC-COA-atom50" elementType="P" x2="-0.11371" y2="-0.04013"/> <atom id="SUC-COA-atom51" elementType="C" x2="0.45151" y2="0.13378"/> <atom id="SUC-COA-atom52" elementType="C" x2="-1.0" y2="-0.59197"/> <atom id="SUC-COA-atom53" elementType="C" x2="-0.74916" y2="-0.14381"/> <atom id="SUC-COA-atom54" elementType="C" x2="0.55184" y2="-0.04013"/> <atom id="SUC-COA-atom55" elementType="C" x2="0.55184" y2="-0.23077"/> <atom id="SUC-COA-atom56" elementType="O" x2="0.64214" y2="-0.82274"/> <atom id="SUC-COA-atom57" elementType="C" x2="0.61873" y2="-0.35452"/> <atom id="SUC-COA-atom58" elementType="N" x2="0.58863" y2="0.55518"/> <atom id="SUC-COA-atom59" elementType="H" x2="0.88294" y2="-0.33779"/> </atomArray> <bondArray> <bond id="SUC-COA-bond1" atomRefs="SUC-COA-atom59 SUC-COA-atom1" order="1"/> <bond id="SUC-COA-bond2" atomRefs="SUC-COA-atom58 SUC-COA-atom24" order="1"/> <bond id="SUC-COA-bond3" atomRefs="SUC-COA-atom57 SUC-COA-atom29" order="1"/> <bond id="SUC-COA-bond4" atomRefs="SUC-COA-atom57 SUC-COA-atom3" order="1"/> <bond id="SUC-COA-bond5" atomRefs="SUC-COA-atom56 SUC-COA-atom7" order="2"/> <bond id="SUC-COA-bond6" atomRefs="SUC-COA-atom55 SUC-COA-atom14" order="1"/> <bond id="SUC-COA-bond7" atomRefs="SUC-COA-atom55 SUC-COA-atom57" order="1"/> <bond id="SUC-COA-bond8" atomRefs="SUC-COA-atom54 SUC-COA-atom55" order="1"/> <bond id="SUC-COA-bond9" atomRefs="SUC-COA-atom53 SUC-COA-atom26" order="1"/> <bond id="SUC-COA-bond10" atomRefs="SUC-COA-atom52 SUC-COA-atom2" order="1"/> <bond id="SUC-COA-bond11" atomRefs="SUC-COA-atom51 SUC-COA-atom5" order="A"/> <bond id="SUC-COA-bond12" atomRefs="SUC-COA-atom50 SUC-COA-atom33" order="1"/> <bond id="SUC-COA-bond13" atomRefs="SUC-COA-atom49 SUC-COA-atom53" order="1"/> <bond id="SUC-COA-bond14" atomRefs="SUC-COA-atom27 SUC-COA-atom48" order="A"/> <bond id="SUC-COA-bond15" atomRefs="SUC-COA-atom47 SUC-COA-atom43" order="1"/> <bond id="SUC-COA-bond16" atomRefs="SUC-COA-atom46 SUC-COA-atom55" order="1"/> <bond id="SUC-COA-bond17" atomRefs="SUC-COA-atom45 SUC-COA-atom10" order="A"/> <bond id="SUC-COA-bond18" atomRefs="SUC-COA-atom39 SUC-COA-atom45" order="A"/> <bond id="SUC-COA-bond19" atomRefs="SUC-COA-atom44 SUC-COA-atom52" order="1"/> <bond id="SUC-COA-bond20" atomRefs="SUC-COA-atom43 SUC-COA-atom54" order="1"/> <bond id="SUC-COA-bond21" atomRefs="SUC-COA-atom42 SUC-COA-atom13" order="1"/> <bond id="SUC-COA-bond22" atomRefs="SUC-COA-atom41 SUC-COA-atom18" order="2"/> <bond id="SUC-COA-bond23" atomRefs="SUC-COA-atom40 SUC-COA-atom16" order="1"/> <bond id="SUC-COA-bond24" atomRefs="SUC-COA-atom48 SUC-COA-atom39" order="A"/> <bond id="SUC-COA-bond25" atomRefs="SUC-COA-atom38 SUC-COA-atom20" order="1"/> <bond id="SUC-COA-bond26" atomRefs="SUC-COA-atom37 SUC-COA-atom40" order="1"/> <bond id="SUC-COA-bond27" atomRefs="SUC-COA-atom36 SUC-COA-atom37" order="1"/> <bond id="SUC-COA-bond28" atomRefs="SUC-COA-atom35 SUC-COA-atom7" order="1"/> <bond id="SUC-COA-bond29" atomRefs="SUC-COA-atom34 SUC-COA-atom50" order="1"/> <bond id="SUC-COA-bond30" atomRefs="SUC-COA-atom33 SUC-COA-atom47" order="1"/> <bond id="SUC-COA-bond31" atomRefs="SUC-COA-atom32 SUC-COA-atom17" order="1"/> <bond id="SUC-COA-bond32" atomRefs="SUC-COA-atom31 SUC-COA-atom57" order="1"/> <bond id="SUC-COA-bond33" atomRefs="SUC-COA-atom30 SUC-COA-atom50" order="2"/> <bond id="SUC-COA-bond34" atomRefs="SUC-COA-atom28 SUC-COA-atom26" order="1"/> <bond id="SUC-COA-bond35" atomRefs="SUC-COA-atom26 SUC-COA-atom32" order="1"/> <bond id="SUC-COA-bond36" atomRefs="SUC-COA-atom25 SUC-COA-atom47" order="1"/> <bond id="SUC-COA-bond37" atomRefs="SUC-COA-atom39 SUC-COA-atom24" order="A"/> <bond id="SUC-COA-bond38" atomRefs="SUC-COA-atom24 SUC-COA-atom12" order="A"/> <bond id="SUC-COA-bond39" atomRefs="SUC-COA-atom23 SUC-COA-atom3" order="1"/> <bond id="SUC-COA-bond40" atomRefs="SUC-COA-atom22 SUC-COA-atom44" order="1"/> <bond id="SUC-COA-bond41" atomRefs="SUC-COA-atom21 SUC-COA-atom47" order="2"/> <bond id="SUC-COA-bond42" atomRefs="SUC-COA-atom20 SUC-COA-atom42" order="1"/> <bond id="SUC-COA-bond43" atomRefs="SUC-COA-atom19 SUC-COA-atom20" order="2"/> <bond id="SUC-COA-bond44" atomRefs="SUC-COA-atom18 SUC-COA-atom36" order="1"/> <bond id="SUC-COA-bond45" atomRefs="SUC-COA-atom17 SUC-COA-atom50" order="1"/> <bond id="SUC-COA-bond46" atomRefs="SUC-COA-atom16 SUC-COA-atom22" order="1"/> <bond id="SUC-COA-bond47" atomRefs="SUC-COA-atom15 SUC-COA-atom22" order="2"/> <bond id="SUC-COA-bond48" atomRefs="SUC-COA-atom14 SUC-COA-atom1" order="1"/> <bond id="SUC-COA-bond49" atomRefs="SUC-COA-atom13 SUC-COA-atom18" order="1"/> <bond id="SUC-COA-bond50" atomRefs="SUC-COA-atom12 SUC-COA-atom51" order="A"/> <bond id="SUC-COA-bond51" atomRefs="SUC-COA-atom11 SUC-COA-atom7" order="1"/> <bond id="SUC-COA-bond52" atomRefs="SUC-COA-atom10 SUC-COA-atom27" order="A"/> <bond id="SUC-COA-bond53" atomRefs="SUC-COA-atom9 SUC-COA-atom3" order="1"/> <bond id="SUC-COA-bond54" atomRefs="SUC-COA-atom8 SUC-COA-atom53" order="1"/> <bond id="SUC-COA-bond55" atomRefs="SUC-COA-atom7 SUC-COA-atom29" order="1"/> <bond id="SUC-COA-bond56" atomRefs="SUC-COA-atom6 SUC-COA-atom8" order="2"/> <bond id="SUC-COA-bond57" atomRefs="SUC-COA-atom5 SUC-COA-atom48" order="A"/> <bond id="SUC-COA-bond58" atomRefs="SUC-COA-atom4 SUC-COA-atom26" order="1"/> <bond id="SUC-COA-bond59" atomRefs="SUC-COA-atom2 SUC-COA-atom8" order="1"/> <bond id="SUC-COA-bond60" atomRefs="SUC-COA-atom1 SUC-COA-atom27" order="1"/> <bond id="SUC-COA-bond61" atomRefs="SUC-COA-atom1 SUC-COA-atom3" order="1"/> </bondArray> <formula concise="C 25 H 40 N 7 O 19 P 3 S 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">867.608</float> <string title="smiles">[CH]3(n1(c2(c(nc1)c(N)ncn2)))(O[CH]([CH]([CH](O)3)OP(O)(=O)O)COP(=O)(O)OP(=O)(O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCSC(=O)CCC(O)=O)</string> <string title="systematicName">Coenzyme A, S-(hydrogen butanedioate)</string> </molecule> </cml> succinyl-CoA 867.6079711914062 suc-co-A succ-S-CoA succinylcoenzyme-A CAS 604-98-8 succinyl-S-CoA ACTIVATION-ALLOSTERIC adenylate CAS 61-19-8 adenylic acid CML <cml> <molecule id="AMP" title="AMP" dictRef="dictAMP"> <atomArray> <atom id="AMP-atom1" elementType="O" x2="0.45706" y2="-1.0"/> <atom id="AMP-atom2" elementType="O" x2="0.25153" y2="0.00307"/> <atom id="AMP-atom3" elementType="C" x2="0.41718" y2="-0.2362"/> <atom id="AMP-atom4" elementType="N" x2="-1.0" y2="-0.25767"/> <atom id="AMP-atom5" elementType="N" x2="-0.15951" y2="-0.25767"/> <atom id="AMP-atom6" elementType="H" x2="0.56442" y2="-0.32822"/> <atom id="AMP-atom7" elementType="N" x2="-0.16258" y2="0.2454"/> <atom id="AMP-atom8" elementType="C" x2="0.70859" y2="0.15031"/> <atom id="AMP-atom9" elementType="C" x2="-0.57055" y2="-0.0184"/> <atom id="AMP-atom10" elementType="C" x2="0.42025" y2="0.2454"/> <atom id="AMP-atom11" elementType="C" x2="0.70859" y2="-0.14417"/> <atom id="AMP-atom12" elementType="N" x2="-0.57669" y2="-0.49693"/> <atom id="AMP-atom13" elementType="O" x2="0.09509" y2="-0.58282"/> <atom id="AMP-atom14" elementType="C" x2="-0.41718" y2="0.41104"/> <atom id="AMP-atom15" elementType="O" x2="0.99693" y2="-0.14417"/> <atom id="AMP-atom16" elementType="O" x2="0.98466" y2="0.23006"/> <atom id="AMP-atom17" elementType="C" x2="-0.30061" y2="-0.0184"/> <atom id="AMP-atom18" elementType="C" x2="-0.71166" y2="-0.25767"/> <atom id="AMP-atom19" elementType="P" x2="0.26994" y2="-0.78221"/> <atom id="AMP-atom20" elementType="N" x2="-0.67485" y2="0.22086"/> <atom id="AMP-atom21" elementType="H" x2="0.42025" y2="0.41718"/> <atom id="AMP-atom22" elementType="C" x2="-0.29755" y2="-0.49693"/> <atom id="AMP-atom23" elementType="O" x2="0.5" y2="-0.60736"/> <atom id="AMP-atom24" elementType="C" x2="0.09509" y2="-0.33742"/> <atom id="AMP-atom25" elementType="O" x2="0.02761" y2="-0.93865"/> </atomArray> <bondArray> <bond id="AMP-bond1" atomRefs="AMP-atom25 AMP-atom19" order="1"/> <bond id="AMP-bond2" atomRefs="AMP-atom23 AMP-atom19" order="2"/> <bond id="AMP-bond3" atomRefs="AMP-atom22 AMP-atom5" order="A"/> <bond id="AMP-bond4" atomRefs="AMP-atom9 AMP-atom20" order="A"/> <bond id="AMP-bond5" atomRefs="AMP-atom20 AMP-atom14" order="A"/> <bond id="AMP-bond6" atomRefs="AMP-atom19 AMP-atom13" order="1"/> <bond id="AMP-bond7" atomRefs="AMP-atom18 AMP-atom12" order="A"/> <bond id="AMP-bond8" atomRefs="AMP-atom9 AMP-atom18" order="A"/> <bond id="AMP-bond9" atomRefs="AMP-atom7 AMP-atom17" order="A"/> <bond id="AMP-bond10" atomRefs="AMP-atom14 AMP-atom7" order="A"/> <bond id="AMP-bond11" atomRefs="AMP-atom13 AMP-atom24" order="1"/> <bond id="AMP-bond12" atomRefs="AMP-atom12 AMP-atom22" order="A"/> <bond id="AMP-bond13" atomRefs="AMP-atom11 AMP-atom15" order="1"/> <bond id="AMP-bond14" atomRefs="AMP-atom11 AMP-atom8" order="1"/> <bond id="AMP-bond15" atomRefs="AMP-atom10 AMP-atom21" order="1"/> <bond id="AMP-bond16" atomRefs="AMP-atom10 AMP-atom7" order="1"/> <bond id="AMP-bond17" atomRefs="AMP-atom17 AMP-atom9" order="A"/> <bond id="AMP-bond18" atomRefs="AMP-atom8 AMP-atom16" order="1"/> <bond id="AMP-bond19" atomRefs="AMP-atom8 AMP-atom10" order="1"/> <bond id="AMP-bond20" atomRefs="AMP-atom5 AMP-atom17" order="A"/> <bond id="AMP-bond21" atomRefs="AMP-atom4 AMP-atom18" order="1"/> <bond id="AMP-bond22" atomRefs="AMP-atom3 AMP-atom11" order="1"/> <bond id="AMP-bond23" atomRefs="AMP-atom3 AMP-atom6" order="1"/> <bond id="AMP-bond24" atomRefs="AMP-atom3 AMP-atom24" order="1"/> <bond id="AMP-bond25" atomRefs="AMP-atom3 AMP-atom2" order="1"/> <bond id="AMP-bond26" atomRefs="AMP-atom2 AMP-atom10" order="1"/> <bond id="AMP-bond27" atomRefs="AMP-atom1 AMP-atom19" order="1"/> </bondArray> <formula concise="C 10 H 14 N 5 O 7 P 1" formalCharge="-2"/> <float title="molecularWeight" units="g/mol">347.224</float> <string title="smiles">[CH]1(O[CH](C(O)C(O)1)COP(=O)(O)O)n2(c3(c(nc2)c(N)ncn3))</string> </molecule> </cml> adenosine-5'-phosphate 347.2239990234375 A adenosine-phosphate AMP adenosine-monophosphate 1.0 ACTIVATION-ALLOSTERIC 1.0 vanadate Vanadate strongly inhibits the enzyme. |CITS: [99364512]| INHIBITION-UNKMECH D-phosphoglycerate 2,3-phosphomutase 2 PGAM2 GPMB-MONOMER Ortholog EcoO157Cyc PIR b4395 SWISS-PROT P36942 PGAM2-MONOMER B4395 RefSeq NP_418812 The enzyme has not been characterized and the subunit structure is unknown. However, phosphoglycerate mutase 1 is a homodimer. SWISS-MODEL P36942 GpmB YtjC MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVATRAKELGITHIISSDLGRTRRTAEIIAQACGCDIIFDSRLRELNMGVLEKRHIDSLTEEEENWRRQLVNGTVDGRIPEGESMQELSDRVNAALESCRDLPQGSRPLLVSHGIALGCLVSTILGLPAWAERRLRLRNCSISRVDYQESLWLASGWVVETAGDISHLDAPALDELQR REVERSIBLE phosphoglyceromutase 2 BPG-dependent PGAM2 E. coli contains three phosphoglycerate mutases. Two are 2,3-bisphosphoglyerate-dependent enzymes, encoded by the gpmA and gpmB genes. The third is a 2,3-bisphosphoglyerate-independent enzyme encoded by the pgmI gene. |CITS: [99364512]| phosphoglycerate mutase 2 phosphoglycerate phosphomutase 2 EcoO157Cyc Ortholog GAPA-MONOMER Vignais ML PubMed Seta FD J Bacteriol 1997;179(16);5218-21 Characterization of Escherichia coli strains with gapA and gapB genes deleted. 1997 Boschi-Muller S 9260967 Branlant G glyceraldehyde 3-phosphate oxidation TRIOSEPHOSPHATE DEHYDROGENASE 1 PO<SUB>4</SUB><SUP>3-</SUP> CAS 14265-44-2 phosphate-inorganic inorganic phosphate orthophosphate Pi phosphate HPO<SUB>4</SUB><SUP>2-</SUP> 94.97100067138672 <cml> <molecule id="Pi" title="phosphate" dictRef="dictPi"> <atomArray> <atom id="Pi-atom1" elementType="P" x2="-0.00166" y2="-0.00166"/> <atom id="Pi-atom2" elementType="O" x2="0.99667" y2="-0.00166" formalCharge="-1"/> <atom id="Pi-atom3" elementType="O" x2="-0.00166" y2="0.99667" formalCharge="-1"/> <atom id="Pi-atom4" elementType="O" x2="-0.00166" y2="-1.0" formalCharge="-1"/> <atom id="Pi-atom5" elementType="O" x2="-1.0" y2="-0.00166"/> </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="O 4 P 1" formalCharge="-3"/> <float title="molecularWeight" units="g/mol">94.971</float> <string title="smiles">P([O-1])([O-1])(=O)[O-1]</string> </molecule> </cml> CML 1 NAD-reduced NADH2 NADH NADH+H+ NADH₂ <cml> <molecule id="NADH" title="NADH" dictRef="dictNADH"> <atomArray> <atom id="NADH-atom1" elementType="C" x2="0.34285715" y2="-0.7542857"/> <atom id="NADH-atom2" elementType="C" x2="0.92" y2="-0.45142856"/> <atom id="NADH-atom3" elementType="H" x2="0.37142858" y2="-0.89428574"/> <atom id="NADH-atom4" elementType="O" x2="0.08285714" y2="-0.64"/> <atom id="NADH-atom5" elementType="O" x2="0.08285714" y2="-0.8657143"/> <atom id="NADH-atom6" elementType="C" x2="0.42857143" y2="-0.93142855"/> <atom id="NADH-atom7" elementType="C" x2="-0.5914286" y2="-0.36"/> <atom id="NADH-atom8" elementType="C" x2="-0.78571427" y2="-0.4342857"/> <atom id="NADH-atom9" elementType="H" x2="-0.48857144" y2="-0.70285714"/> <atom id="NADH-atom10" elementType="H" x2="0.7" y2="-0.34285715"/> <atom id="NADH-atom11" elementType="O" x2="0.42857143" y2="-1.0"/> <atom id="NADH-atom12" elementType="C" x2="0.52" y2="-0.46285716"/> <atom id="NADH-atom13" elementType="C" x2="-1.0" y2="-0.4342857"/> <atom id="NADH-atom14" elementType="H" x2="0.42857143" y2="-0.86285716"/> <atom id="NADH-atom15" elementType="H" x2="-0.68" y2="-0.7542857"/> <atom id="NADH-atom16" elementType="H" x2="0.6028572" y2="-0.34571427"/> <atom id="NADH-atom17" elementType="C" x2="-0.42285714" y2="-0.68285716"/> <atom id="NADH-atom18" elementType="C" x2="0.7714286" y2="-0.45142856"/> <atom id="NADH-atom19" elementType="H" x2="0.6457143" y2="-0.89428574"/> <atom id="NADH-atom20" elementType="O" x2="-0.5542857" y2="-0.61142856"/> <atom id="NADH-atom21" elementType="C" x2="0.6457143" y2="-0.82857144"/> <atom id="NADH-atom22" elementType="O" x2="-0.48857144" y2="-0.8428571"/> <atom id="NADH-atom23" elementType="C" x2="0.37142858" y2="-0.82857144"/> <atom id="NADH-atom24" elementType="C" x2="0.52" y2="-0.6085714"/> <atom id="NADH-atom25" elementType="C" x2="-0.48857144" y2="-0.77428573"/> <atom id="NADH-atom26" elementType="C" x2="-0.61714286" y2="-0.77428573"/> <atom id="NADH-atom27" elementType="O" x2="0.5" y2="-0.7457143"/> <atom id="NADH-atom28" elementType="N" x2="-0.8971428" y2="-0.13142857"/> <atom id="NADH-atom29" elementType="O" x2="0.21428572" y2="-0.7542857"/> <atom id="NADH-atom30" elementType="O" x2="-0.17714286" y2="-0.64"/> <atom id="NADH-atom31" elementType="N" x2="-1.0" y2="-0.31142858"/> <atom id="NADH-atom32" elementType="N" x2="-0.68" y2="-0.48285714"/> <atom id="NADH-atom33" elementType="N" x2="0.9942857" y2="-0.5342857"/> <atom id="NADH-atom34" elementType="C" x2="0.7714286" y2="-0.6085714"/> <atom id="NADH-atom35" elementType="C" x2="-0.78571427" y2="-0.31142858"/> <atom id="NADH-atom36" elementType="H" x2="0.5714286" y2="-0.86285716"/> <atom id="NADH-atom37" elementType="P" x2="0.08285714" y2="-0.7542857"/> <atom id="NADH-atom38" elementType="O" x2="-0.61714286" y2="-0.8428571"/> <atom id="NADH-atom39" elementType="N" x2="-0.68" y2="-0.25714287"/> <atom id="NADH-atom40" elementType="P" x2="-0.17714286" y2="-0.7542857"/> <atom id="NADH-atom41" elementType="C" x2="-0.68" y2="-0.68285716"/> <atom id="NADH-atom42" elementType="N" x2="0.6457143" y2="-0.67714286"/> <atom id="NADH-atom43" elementType="H" x2="-0.61714286" y2="-0.70285714"/> <atom id="NADH-atom44" elementType="O" x2="0.99714285" y2="-0.37142858"/> <atom id="NADH-atom45" elementType="N" x2="-0.8971428" y2="-0.48857144"/> <atom id="NADH-atom46" elementType="C" x2="-0.36857143" y2="-0.7657143"/> <atom id="NADH-atom47" elementType="O" x2="0.5714286" y2="-1.0"/> <atom id="NADH-atom48" elementType="O" x2="-0.17714286" y2="-0.8657143"/> <atom id="NADH-atom49" elementType="C" x2="-0.8971428" y2="-0.24857143"/> <atom id="NADH-atom50" elementType="O" x2="-0.2742857" y2="-0.7542857"/> <atom id="NADH-atom51" elementType="H" x2="-0.42285714" y2="-0.61714286"/> <atom id="NADH-atom52" elementType="O" x2="-0.042857144" y2="-0.7542857"/> <atom id="NADH-atom53" elementType="C" x2="0.5714286" y2="-0.93142855"/> <atom id="NADH-atom54" elementType="C" x2="0.6542857" y2="-0.39142856"/> </atomArray> <bondArray> <bond id="NADH-bond1" atomRefs="NADH-atom54 NADH-atom18" order="1"/> <bond id="NADH-bond2" atomRefs="NADH-atom53 NADH-atom6" order="1"/> <bond id="NADH-bond3" atomRefs="NADH-atom52 NADH-atom40" order="1"/> <bond id="NADH-bond4" atomRefs="NADH-atom51 NADH-atom17" order="1"/> <bond id="NADH-bond5" atomRefs="NADH-atom50 NADH-atom46" order="1"/> <bond id="NADH-bond6" atomRefs="NADH-atom49 NADH-atom31" order="A"/> <bond id="NADH-bond7" atomRefs="NADH-atom48 NADH-atom40" order="1"/> <bond id="NADH-bond8" atomRefs="NADH-atom47 NADH-atom53" order="1"/> <bond id="NADH-bond9" atomRefs="NADH-atom46 NADH-atom17" order="1"/> <bond id="NADH-bond10" atomRefs="NADH-atom45 NADH-atom8" order="A"/> <bond id="NADH-bond11" atomRefs="NADH-atom44 NADH-atom2" order="2"/> <bond id="NADH-bond12" atomRefs="NADH-atom43 NADH-atom26" order="1"/> <bond id="NADH-bond13" atomRefs="NADH-atom42 NADH-atom21" order="1"/> <bond id="NADH-bond14" atomRefs="NADH-atom42 NADH-atom24" order="1"/> <bond id="NADH-bond15" atomRefs="NADH-atom41 NADH-atom32" order="1"/> <bond id="NADH-bond16" atomRefs="NADH-atom41 NADH-atom26" order="1"/> <bond id="NADH-bond17" atomRefs="NADH-atom40 NADH-atom50" order="1"/> <bond id="NADH-bond18" atomRefs="NADH-atom39 NADH-atom35" order="A"/> <bond id="NADH-bond19" atomRefs="NADH-atom38 NADH-atom26" order="1"/> <bond id="NADH-bond20" atomRefs="NADH-atom37 NADH-atom52" order="1"/> <bond id="NADH-bond21" atomRefs="NADH-atom36 NADH-atom53" order="1"/> <bond id="NADH-bond22" atomRefs="NADH-atom35 NADH-atom49" order="A"/> <bond id="NADH-bond23" atomRefs="NADH-atom35 NADH-atom8" order="A"/> <bond id="NADH-bond24" atomRefs="NADH-atom34 NADH-atom42" order="1"/> <bond id="NADH-bond25" atomRefs="NADH-atom33 NADH-atom2" order="1"/> <bond id="NADH-bond26" atomRefs="NADH-atom32 NADH-atom7" order="A"/> <bond id="NADH-bond27" atomRefs="NADH-atom31 NADH-atom13" order="A"/> <bond id="NADH-bond28" atomRefs="NADH-atom30 NADH-atom40" order="2"/> <bond id="NADH-bond29" atomRefs="NADH-atom29 NADH-atom37" order="1"/> <bond id="NADH-bond30" atomRefs="NADH-atom28 NADH-atom49" order="1"/> <bond id="NADH-bond31" atomRefs="NADH-atom27 NADH-atom23" order="1"/> <bond id="NADH-bond32" atomRefs="NADH-atom25 NADH-atom26" order="1"/> <bond id="NADH-bond33" atomRefs="NADH-atom23 NADH-atom1" order="1"/> <bond id="NADH-bond34" atomRefs="NADH-atom23 NADH-atom6" order="1"/> <bond id="NADH-bond35" atomRefs="NADH-atom22 NADH-atom25" order="1"/> <bond id="NADH-bond36" atomRefs="NADH-atom21 NADH-atom27" order="1"/> <bond id="NADH-bond37" atomRefs="NADH-atom21 NADH-atom53" order="1"/> <bond id="NADH-bond38" atomRefs="NADH-atom20 NADH-atom41" order="1"/> <bond id="NADH-bond39" atomRefs="NADH-atom19 NADH-atom21" order="1"/> <bond id="NADH-bond40" atomRefs="NADH-atom18 NADH-atom34" order="2"/> <bond id="NADH-bond41" atomRefs="NADH-atom17 NADH-atom20" order="1"/> <bond id="NADH-bond42" atomRefs="NADH-atom17 NADH-atom25" order="1"/> <bond id="NADH-bond43" atomRefs="NADH-atom16 NADH-atom54" order="1"/> <bond id="NADH-bond44" atomRefs="NADH-atom15 NADH-atom41" order="1"/> <bond id="NADH-bond45" atomRefs="NADH-atom14 NADH-atom6" order="1"/> <bond id="NADH-bond46" atomRefs="NADH-atom13 NADH-atom45" order="A"/> <bond id="NADH-bond47" atomRefs="NADH-atom12 NADH-atom24" order="2"/> <bond id="NADH-bond48" atomRefs="NADH-atom12 NADH-atom54" order="1"/> <bond id="NADH-bond49" atomRefs="NADH-atom11 NADH-atom6" order="1"/> <bond id="NADH-bond50" atomRefs="NADH-atom10 NADH-atom54" order="1"/> <bond id="NADH-bond51" atomRefs="NADH-atom9 NADH-atom25" order="1"/> <bond id="NADH-bond52" atomRefs="NADH-atom8 NADH-atom32" order="A"/> <bond id="NADH-bond53" atomRefs="NADH-atom7 NADH-atom39" order="A"/> <bond id="NADH-bond54" atomRefs="NADH-atom5 NADH-atom37" order="1"/> <bond id="NADH-bond55" atomRefs="NADH-atom4 NADH-atom37" order="2"/> <bond id="NADH-bond56" atomRefs="NADH-atom3 NADH-atom23" order="1"/> <bond id="NADH-bond57" atomRefs="NADH-atom2 NADH-atom18" order="1"/> <bond id="NADH-bond58" atomRefs="NADH-atom1 NADH-atom29" order="1"/> </bondArray> <formula concise="C 21 H 29 N 7 O 14 P 2" formalCharge="0"/> <float title="molecularWeight" units="g/mol">665.446</float> <string title="smiles">C([CH]1(O[CH]([CH](O)[CH]1O)N2(C=C(C(=O)N)[CH2]C=C2)))OP(=O)(O)OP(=O)(O)OC[CH]3(O[CH]([CH](O)[CH](O)3)n4(c5(c(nc4)c(N)ncn5)))</string> </molecule> </cml> CML DPNH dihydrodiphosphopyridine nucleotide nicotinamide adenine dinucleotide reduced dihydronicotinamide adenine dinucleotide diphosphopyridine nucleotide reduced 665.4459838867188 1 glyceraldehyde-phosphate 142-10-9 CAS glyceraldehyde-3-P 3-phosphoglyceraldehyde glyceraldehyde-3-phosphate D-glyceraldehyde-3-phosphate D-glyceraldehyde-3-P gap CML <cml> <molecule id="GAP" title="glyceraldehyde-3-phosphate" dictRef="dictGAP"> <atomArray> <atom id="GAP-atom1" elementType="C" x2="-1.0" y2="-0.54088"/> <atom id="GAP-atom2" elementType="P" x2="-0.1478" y2="0.53774"/> <atom id="GAP-atom3" elementType="O" x2="-0.13836" y2="-0.2044"/> <atom id="GAP-atom4" elementType="O" x2="0.31132" y2="0.53774"/> <atom id="GAP-atom5" elementType="O" x2="-0.1478" y2="0.07862"/> <atom id="GAP-atom6" elementType="O" x2="-1.0" y2="-1.0"/> <atom id="GAP-atom7" elementType="O" x2="-0.1478" y2="0.99686"/> <atom id="GAP-atom8" elementType="C" x2="-1.0" y2="0.1761"/> <atom id="GAP-atom9" elementType="O" x2="-0.59748" y2="0.53774"/> <atom id="GAP-atom10" elementType="C" x2="-0.59748" y2="-0.2044"/> </atomArray> <bondArray> <bond id="GAP-bond1" atomRefs="GAP-atom10 GAP-atom3" order="1"/> <bond id="GAP-bond2" atomRefs="GAP-atom10 GAP-atom8" order="1"/> <bond id="GAP-bond3" atomRefs="GAP-atom9 GAP-atom2" order="1"/> <bond id="GAP-bond4" atomRefs="GAP-atom8 GAP-atom9" order="1"/> <bond id="GAP-bond5" atomRefs="GAP-atom6 GAP-atom1" order="2"/> <bond id="GAP-bond6" atomRefs="GAP-atom2 GAP-atom5" order="1"/> <bond id="GAP-bond7" atomRefs="GAP-atom2 GAP-atom7" order="1"/> <bond id="GAP-bond8" atomRefs="GAP-atom2 GAP-atom4" order="2"/> <bond id="GAP-bond9" atomRefs="GAP-atom1 GAP-atom10" order="1"/> </bondArray> <formula concise="C 3 H 7 O 6 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">170.058</float> <string title="smiles">C(=O)C(O)COP(O)(O)=O</string> </molecule> </cml> glyceraldehyde-P 170.05799865722656 1.2.1.12 GAPDH 1.5 1 663.4299926757812 nicotinamide adenine dinucleotide nicotinamide adenine dinucleotide oxidized NAD+ diphosphopyridine nucleotide NAD-ox <cml> <molecule id="NAD" title="NAD" dictRef="dictNAD"> <atomArray> <atom id="NAD-atom1" elementType="C" x2="-0.35491604" y2="-0.73141485"/> <atom id="NAD-atom2" elementType="N" x2="0.6834533" y2="-0.64028776" formalCharge="1"/> <atom id="NAD-atom3" elementType="C" x2="-0.7793765" y2="-0.2589928"/> <atom id="NAD-atom4" elementType="N" x2="-0.67146283" y2="-0.41246998"/> <atom id="NAD-atom5" elementType="H" x2="-0.6618705" y2="-0.7050359"/> <atom id="NAD-atom6" elementType="C" x2="0.45803356" y2="-0.9256595"/> <atom id="NAD-atom7" elementType="O" x2="-0.016786575" y2="-0.71702635"/> <atom id="NAD-atom8" elementType="O" x2="0.6139089" y2="-1.0"/> <atom id="NAD-atom9" elementType="O" x2="-0.58752996" y2="-0.7865707"/> <atom id="NAD-atom10" elementType="C" x2="0.6906475" y2="-0.34532374"/> <atom id="NAD-atom11" elementType="C" x2="-1.0" y2="-0.3860911"/> <atom id="NAD-atom12" elementType="O" x2="-0.5467626" y2="-0.5707434"/> <atom id="NAD-atom13" elementType="C" x2="0.37649882" y2="-0.71702635"/> <atom id="NAD-atom14" elementType="P" x2="-0.15347719" y2="-0.71702635"/> <atom id="NAD-atom15" elementType="O" x2="0.24460435" y2="-0.71702635"/> <atom id="NAD-atom16" elementType="C" x2="-0.8920863" y2="-0.1966427"/> <atom id="NAD-atom17" elementType="C" x2="-0.4028777" y2="-0.6522782"/> <atom id="NAD-atom18" elementType="O" x2="-0.15347719" y2="-0.5971223"/> <atom id="NAD-atom19" elementType="O" x2="-0.47961628" y2="-0.7865707"/> <atom id="NAD-atom20" elementType="C" x2="0.6139089" y2="-0.9256595"/> <atom id="NAD-atom21" elementType="N" x2="-0.8920863" y2="-0.076738596"/> <atom id="NAD-atom22" elementType="H" x2="0.6139089" y2="-0.853717"/> <atom id="NAD-atom23" elementType="H" x2="-0.58752996" y2="-0.64028776"/> <atom id="NAD-atom24" elementType="C" x2="-0.5851319" y2="-0.31414866"/> <atom id="NAD-atom25" elementType="H" x2="0.45803356" y2="-0.853717"/> <atom id="NAD-atom26" elementType="C" x2="0.96642685" y2="-0.40527576"/> <atom id="NAD-atom27" elementType="C" x2="-0.67146283" y2="-0.6354916"/> <atom id="NAD-atom28" elementType="C" x2="0.556355" y2="-0.5683453"/> <atom id="NAD-atom29" elementType="H" x2="-0.4028777" y2="-0.5779376"/> <atom id="NAD-atom30" elementType="N" x2="-1.0" y2="-0.2589928"/> <atom id="NAD-atom31" elementType="C" x2="0.6834533" y2="-0.8057554"/> <atom id="NAD-atom32" elementType="C" x2="0.37649882" y2="-0.8057554"/> <atom id="NAD-atom33" elementType="H" x2="0.37649882" y2="-0.8800959"/> <atom id="NAD-atom34" elementType="O" x2="-0.25659472" y2="-0.71702635"/> <atom id="NAD-atom35" elementType="O" x2="-0.15347719" y2="-0.83693045"/> <atom id="NAD-atom36" elementType="O" x2="0.53237414" y2="-0.7505995"/> <atom id="NAD-atom37" elementType="C" x2="-0.58752996" y2="-0.7146283"/> <atom id="NAD-atom38" elementType="C" x2="0.8153478" y2="-0.42206234"/> <atom id="NAD-atom39" elementType="C" x2="0.8153478" y2="-0.5683453"/> <atom id="NAD-atom40" elementType="O" x2="0.45803356" y2="-1.0"/> <atom id="NAD-atom41" elementType="O" x2="0.10791373" y2="-0.83693045" formalCharge="-1"/> <atom id="NAD-atom42" elementType="O" x2="0.96642685" y2="-0.28537166"/> <atom id="NAD-atom43" elementType="P" x2="0.10791373" y2="-0.71702635"/> <atom id="NAD-atom44" elementType="N" x2="-0.8920863" y2="-0.4484412"/> <atom id="NAD-atom45" elementType="C" x2="-0.47961628" y2="-0.7146283"/> <atom id="NAD-atom46" elementType="H" x2="-0.47961628" y2="-0.64028776"/> <atom id="NAD-atom47" elementType="O" x2="0.10791373" y2="-0.5971223"/> <atom id="NAD-atom48" elementType="H" x2="0.6834533" y2="-0.8800959"/> <atom id="NAD-atom49" elementType="C" x2="0.556355" y2="-0.4172662"/> <atom id="NAD-atom50" elementType="N" x2="-0.67146283" y2="-0.20383692"/> <atom id="NAD-atom51" elementType="C" x2="-0.7793765" y2="-0.3860911"/> <atom id="NAD-atom52" elementType="N" x2="0.997602" y2="-0.5203837"/> </atomArray> <bondArray> <bond id="NAD-bond1" atomRefs="NAD-atom52 NAD-atom26" order="1"/> <bond id="NAD-bond2" atomRefs="NAD-atom51 NAD-atom3" order="A"/> <bond id="NAD-bond3" atomRefs="NAD-atom50 NAD-atom24" order="A"/> <bond id="NAD-bond4" atomRefs="NAD-atom49 NAD-atom10" order="A"/> <bond id="NAD-bond5" atomRefs="NAD-atom48 NAD-atom31" order="1"/> <bond id="NAD-bond6" atomRefs="NAD-atom47 NAD-atom43" order="2"/> <bond id="NAD-bond7" atomRefs="NAD-atom46 NAD-atom45" order="1"/> <bond id="NAD-bond8" atomRefs="NAD-atom45 NAD-atom37" order="1"/> <bond id="NAD-bond9" atomRefs="NAD-atom44 NAD-atom51" order="A"/> <bond id="NAD-bond10" atomRefs="NAD-atom43 NAD-atom7" order="1"/> <bond id="NAD-bond11" atomRefs="NAD-atom42 NAD-atom26" order="2"/> <bond id="NAD-bond12" atomRefs="NAD-atom41 NAD-atom43" order="1"/> <bond id="NAD-bond13" atomRefs="NAD-atom40 NAD-atom6" order="1"/> <bond id="NAD-bond14" atomRefs="NAD-atom39 NAD-atom2" order="A"/> <bond id="NAD-bond15" atomRefs="NAD-atom38 NAD-atom39" order="A"/> <bond id="NAD-bond16" atomRefs="NAD-atom36 NAD-atom32" order="1"/> <bond id="NAD-bond17" atomRefs="NAD-atom35 NAD-atom14" order="1"/> <bond id="NAD-bond18" atomRefs="NAD-atom34 NAD-atom1" order="1"/> <bond id="NAD-bond19" atomRefs="NAD-atom33 NAD-atom32" order="1"/> <bond id="NAD-bond20" atomRefs="NAD-atom32 NAD-atom6" order="1"/> <bond id="NAD-bond21" atomRefs="NAD-atom32 NAD-atom13" order="1"/> <bond id="NAD-bond22" atomRefs="NAD-atom31 NAD-atom20" order="1"/> <bond id="NAD-bond23" atomRefs="NAD-atom31 NAD-atom36" order="1"/> <bond id="NAD-bond24" atomRefs="NAD-atom30 NAD-atom11" order="A"/> <bond id="NAD-bond25" atomRefs="NAD-atom29 NAD-atom17" order="1"/> <bond id="NAD-bond26" atomRefs="NAD-atom28 NAD-atom49" order="A"/> <bond id="NAD-bond27" atomRefs="NAD-atom27 NAD-atom37" order="1"/> <bond id="NAD-bond28" atomRefs="NAD-atom27 NAD-atom4" order="1"/> <bond id="NAD-bond29" atomRefs="NAD-atom26 NAD-atom38" order="1"/> <bond id="NAD-bond30" atomRefs="NAD-atom25 NAD-atom6" order="1"/> <bond id="NAD-bond31" atomRefs="NAD-atom24 NAD-atom4" order="A"/> <bond id="NAD-bond32" atomRefs="NAD-atom23 NAD-atom37" order="1"/> <bond id="NAD-bond33" atomRefs="NAD-atom22 NAD-atom20" order="1"/> <bond id="NAD-bond34" atomRefs="NAD-atom21 NAD-atom16" order="1"/> <bond id="NAD-bond35" atomRefs="NAD-atom20 NAD-atom6" order="1"/> <bond id="NAD-bond36" atomRefs="NAD-atom19 NAD-atom45" order="1"/> <bond id="NAD-bond37" atomRefs="NAD-atom18 NAD-atom14" order="2"/> <bond id="NAD-bond38" atomRefs="NAD-atom17 NAD-atom45" order="1"/> <bond id="NAD-bond39" atomRefs="NAD-atom17 NAD-atom12" order="1"/> <bond id="NAD-bond40" atomRefs="NAD-atom16 NAD-atom30" order="A"/> <bond id="NAD-bond41" atomRefs="NAD-atom15 NAD-atom43" order="1"/> <bond id="NAD-bond42" atomRefs="NAD-atom14 NAD-atom34" order="1"/> <bond id="NAD-bond43" atomRefs="NAD-atom13 NAD-atom15" order="1"/> <bond id="NAD-bond44" atomRefs="NAD-atom12 NAD-atom27" order="1"/> <bond id="NAD-bond45" atomRefs="NAD-atom11 NAD-atom44" order="A"/> <bond id="NAD-bond46" atomRefs="NAD-atom10 NAD-atom38" order="A"/> <bond id="NAD-bond47" atomRefs="NAD-atom9 NAD-atom37" order="1"/> <bond id="NAD-bond48" atomRefs="NAD-atom8 NAD-atom20" order="1"/> <bond id="NAD-bond49" atomRefs="NAD-atom7 NAD-atom14" order="1"/> <bond id="NAD-bond50" atomRefs="NAD-atom5 NAD-atom27" order="1"/> <bond id="NAD-bond51" atomRefs="NAD-atom4 NAD-atom51" order="A"/> <bond id="NAD-bond52" atomRefs="NAD-atom3 NAD-atom50" order="A"/> <bond id="NAD-bond53" atomRefs="NAD-atom3 NAD-atom16" order="A"/> <bond id="NAD-bond54" atomRefs="NAD-atom2 NAD-atom31" order="1"/> <bond id="NAD-bond55" atomRefs="NAD-atom2 NAD-atom28" order="A"/> <bond id="NAD-bond56" atomRefs="NAD-atom1 NAD-atom17" 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([CH]1(O[CH]([CH](O)[CH](O)1)n2(c3(c(nc2)c(N)ncn3))))OP(=O)(O)OP([O-1])(=O)OC[CH]4(O[CH]([CH](O)[CH](O)4)[n+1]5(cc(C(N)=O)ccc5))</string> </molecule> </cml> CML NAD diphosphopyridine nucleotide oxidized DPN DPN+ coenzyme I NAD-oxidized DPN-ox 53-84-9 CAS 1 The E.coli sequence contains a certain number of amino acids which are conserved in all GAPDHs so far sequenced and which are postulated to be directly implicated in the NAD+ binding or in the catalysis mechanism. |CITS:[85257641]| There appear to be only two active sites per molecule.|CITS:[79255500]| NAD required for the phosphorylation as well as the oxidation |CITS:[79255500]| REVERSIBLE triosephosphate dehydrogenase glyceraldehyde 3-phosphate dehydrogenase-A complex GAPDH-A 2990926 PubMed Branlant C Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase. 1985 Eur J Biochem 1985;150(1);61-6 Branlant G GAPDH-A-CPLX Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12. Yang Y 9696782 Zhao G 1998 Winkler ME Man TK PubMed J Bacteriol 1998;180(16);4294-9 2124629 PubMed 1990 J Mol Evol 1990;31(5);383-8 Alberro MR A naturally occurring horizontal gene transfer from a eukaryote to a prokaryote. Anderson KL Feng DF Doolittle RF 4 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNKVLDLIAHISK NP_416293 RefSeq B1779 Gap1 SWISS-MODEL P06977 glyceraldehyde 3-phosphate dehydrogenase-A monomer GapA PDB 1GAD Gad A higher degree of sequence homology exists between E.coli and eucaryotic enzymes than betwen E. coli and the thermophilic bacterial enzyme |CITS:[85257641]|. Mutant exhibits a growth defect and also exhibits increased aggregation and lysis that are rescued by high-salt media |CITS: [9260967]|. Regulation has been described |CITS: [12672900]|. The regulation of the fkpA, gapA, and hslT genes is affected by evolution under conditions of chronic heat stress |CITS: [12672900]|. PIR b1779 PDB 1GAE SWISS-PROT P06977 E.coli is unusual in having two glyceraldehyde-3-phosphate dehydrogenases. The protein GAPDH-A has a sequence that is more similar to eukaryotic sequences than it is to prokaryotic types |CITS:[91087241]|. GapA is required for glycolysis, while Epd (GapB) is not |CITS: [9260967]|. GapA and Epd may be involved in production of pyridoxal 5'-phosphate (PLP) |CITS: [9696782]|. The Enzymes, Vol.XIII Academic Press, New York 1976;3rd Edition Oxidation-Reduction, Part C phosphoglycerate phosphorylation In this reaction a phosphoryl group is transferred from the acyl phosphate of 1,3 diphosphoglycerate to ADP thereby forming ATP and 3-phosphoglycerate.|CITS:[90336971]| 2.7.2.3 2,3-diphospho-D-glycerate PGK SWISS-PROT P11665 MSVIKMTDLDLAGKRVFIRADLNVPVKDGKVTSDARIRASLPTIELALKQGAKVMVTSHLGRPTEGEYNEEFSLLPVVNYLKDKLSNPVRLVKDYLDGVDVAEGELVVLENVRFNKGEKKDDETLSKKYAALCDVFVMDAFGTAHRAQASTHGIGKFADVACAGPLLAAELDALGKALKEPARPMVAIVGGSKVSTKLTVLDSLSKIADQLIVGGGIANTFIAAQGHDVGKSLYEADLVDEAKRLLTTCNIPVPSDVRVATEFSETAPATLKSVNDVKADEQILDIGDASAQELAEILKNAKTILWNGPVGVFEFPNFRKGTEIVANAIADSEAFSIAGGGDTLAAIDLFGIADKISYISTGGGAFLEFVEGKVLPAVAMLEERAKK b2926 PIR Phosphoglycerate kinase is one of the proteins induced by anaerobiosis. |CITS:[89306676]| The gene is transcribed from two promoters, one immediately in front of an upstream gene coding for a 38-kDa polypeptide of unknown function. The pgk gene was also found to show growth phase regulation. A structural determinant for glycerate 3-P kinase is located near serA. The map order is speB-pgk-serA-lysA-argA-eno-cysC.|CITS:[76195925]| Pgk has similarity to an <i>Edwardsiella ictaluri</i> protein |CITS: [12542086]|. Pgk NP_417401 RefSeq P11665 SWISS-MODEL B2926 EcoO157Cyc Ortholog G7E-3-MONOMER The structure of Pgk determined crystallographically is best described as an open bi-lobal molecule. The active site of the enzyme lies deep in the cleft formed between the two lobes.|CITS:[90336971]| When purified enzymes were employed there was absolute dependence upon the respective substrates of the glycolytic pathway. There was no activity unless ATP and glycerate-3-P were both included.|CITS:[71230170]| 2-phospho-D-glycerate phosphotransferase REVERSIBLE 3-phosphoglycerate kinase phosphoglycerate kinase Glycerate 3-P kinase ACTIVATION-UNKMECH ACTIVATION-UNKMECH 1.0 AsO<SUB>4</SUB><SUP>3-</SUP> 138.91900634765625 arsenate CML <cml> <molecule id="ARSENATE" title="arsenate" dictRef="dictARSENATE"> <atomArray> <atom id="ARSENATE-atom1" elementType="AS" x2="0.0" y2="0.0"/> <atom id="ARSENATE-atom2" elementType="O" x2="0.9961977" y2="0.0" formalCharge="-1"/> <atom id="ARSENATE-atom3" elementType="O" x2="0.0" y2="0.9961977" formalCharge="-1"/> <atom id="ARSENATE-atom4" elementType="O" x2="0.0" y2="-1.0" formalCharge="-1"/> <atom id="ARSENATE-atom5" elementType="O" x2="-1.0" y2="0.0"/> </atomArray> <bondArray> <bond id="ARSENATE-bond1" atomRefs="ARSENATE-atom5 ARSENATE-atom1" order="2"/> <bond id="ARSENATE-bond2" atomRefs="ARSENATE-atom4 ARSENATE-atom1" order="1"/> <bond id="ARSENATE-bond3" atomRefs="ARSENATE-atom3 ARSENATE-atom1" order="1"/> <bond id="ARSENATE-bond4" atomRefs="ARSENATE-atom2 ARSENATE-atom1" order="1"/> </bondArray> <formula concise="O 4 AS 1" formalCharge="-3"/> <float title="molecularWeight" units="g/mol">138.919</float> <string title="smiles">[As]([O-1])([O-1])(=O)[O-1]</string> </molecule> </cml> inorganic arsenate orthoarsenate ACTIVATION-UNKMECH Winkler ME PubMed J Bacteriol 1995;177(10);2804-12 1995 Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis. Bharani N Pease AJ 7751290 Zhao G 6235149 1984 Gene 1984;28(3);337-42 PubMed Nucleotide sequence of gene pfkB encoding the minor phosphofructokinase of Escherichia coli K-12. Daldal F PfkB 6-phosphofructokinase-2 monomer Ortholog PFKB-MONOMER EcoO157Cyc MVRIYTLTLAPSLDSATITPQIYPEGKLRCTAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADENVPVATVEAKDWTRQNLHVHVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVISGSLPPGVKLEKLTQLISAAQKQGIRCIVDSSGEALSAALAIGNIELVKPNQKELSALVNRELTQPDDVRKAAQEIVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYAYLSR RefSeq NP_416237 SWISS-PROT P06999 B1723 PIR b1723 CAS 56-73-5 1 <cml> <molecule id="DIHYDROXY-ACETONE-PHOSPHATE" title="dihydroxy-acetone-phosphate" dictRef="dictDIHYDROXY-ACETONE-PHOSPHATE"> <atomArray> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom1" elementType="O" x2="0.60784" y2="-1.0"/> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom2" elementType="O" x2="-1.0" y2="-0.53922"/> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom3" elementType="P" x2="0.60784" y2="-0.61111"/> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom4" elementType="O" x2="-0.38562" y2="-0.21242"/> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom5" elementType="C" x2="-0.38562" y2="-0.60131"/> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom6" elementType="O" x2="0.19608" y2="-0.61111"/> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom7" elementType="C" x2="-0.68954" y2="-0.77451"/> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom8" elementType="O" x2="0.99673" y2="-0.61111"/> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom9" elementType="O" x2="0.60784" y2="-0.22222"/> <atom id="DIHYDROXY-ACETONE-PHOSPHATE-atom10" elementType="C" x2="-0.07843" y2="-0.77451"/> </atomArray> <bondArray> <bond id="DIHYDROXY-ACETONE-PHOSPHATE-bond1" atomRefs="DIHYDROXY-ACETONE-PHOSPHATE-atom10 DIHYDROXY-ACETONE-PHOSPHATE-atom6" order="1"/> <bond id="DIHYDROXY-ACETONE-PHOSPHATE-bond2" atomRefs="DIHYDROXY-ACETONE-PHOSPHATE-atom9 DIHYDROXY-ACETONE-PHOSPHATE-atom3" order="2"/> <bond id="DIHYDROXY-ACETONE-PHOSPHATE-bond3" atomRefs="DIHYDROXY-ACETONE-PHOSPHATE-atom8 DIHYDROXY-ACETONE-PHOSPHATE-atom3" order="1"/> <bond id="DIHYDROXY-ACETONE-PHOSPHATE-bond4" atomRefs="DIHYDROXY-ACETONE-PHOSPHATE-atom7 DIHYDROXY-ACETONE-PHOSPHATE-atom5" order="1"/> <bond id="DIHYDROXY-ACETONE-PHOSPHATE-bond5" atomRefs="DIHYDROXY-ACETONE-PHOSPHATE-atom6 DIHYDROXY-ACETONE-PHOSPHATE-atom3" order="1"/> <bond id="DIHYDROXY-ACETONE-PHOSPHATE-bond6" atomRefs="DIHYDROXY-ACETONE-PHOSPHATE-atom5 DIHYDROXY-ACETONE-PHOSPHATE-atom10" order="1"/> <bond id="DIHYDROXY-ACETONE-PHOSPHATE-bond7" atomRefs="DIHYDROXY-ACETONE-PHOSPHATE-atom4 DIHYDROXY-ACETONE-PHOSPHATE-atom5" order="2"/> <bond id="DIHYDROXY-ACETONE-PHOSPHATE-bond8" atomRefs="DIHYDROXY-ACETONE-PHOSPHATE-atom2 DIHYDROXY-ACETONE-PHOSPHATE-atom7" order="1"/> <bond id="DIHYDROXY-ACETONE-PHOSPHATE-bond9" atomRefs="DIHYDROXY-ACETONE-PHOSPHATE-atom1 DIHYDROXY-ACETONE-PHOSPHATE-atom3" order="1"/> </bondArray> <formula concise="C 3 H 7 O 6 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">170.058</float> <string title="smiles">C(O)C(=O)COP(O)(=O)O</string> </molecule> </cml> CML dihydroxy-acetone-phosphate dihydroxyacetone-P 57-04-5 CAS dihydroxyacetone 3-phosphate DHAP dihydroxyacetone-phosphate glycerone-phosphate 170.05799865722656 di-OH-acetone-P 146-91-8 CAS <cml> <molecule id="GDP" title="GDP" dictRef="dictGDP"> <atomArray> <atom id="GDP-atom1" elementType="N" x2="-0.05666667" y2="0.06666667"/> <atom id="GDP-atom2" elementType="H" x2="0.99666667" y2="-0.7366667"/> <atom id="GDP-atom3" elementType="N" x2="0.99666667" y2="0.2"/> <atom id="GDP-atom4" elementType="N" x2="0.4" y2="0.046666667"/> <atom id="GDP-atom5" elementType="N" x2="0.18" y2="0.44"/> <atom id="GDP-atom6" elementType="C" x2="0.26666668" y2="-0.39333335"/> <atom id="GDP-atom7" elementType="C" x2="0.99666667" y2="0.42333335"/> <atom id="GDP-atom8" elementType="O" x2="-0.7266667" y2="-0.12"/> <atom id="GDP-atom9" elementType="N" x2="0.81666666" y2="0.5466667"/> <atom id="GDP-atom10" elementType="O" x2="0.41333333" y2="-1.0"/> <atom id="GDP-atom11" elementType="C" x2="0.62" y2="0.44"/> <atom id="GDP-atom12" elementType="H" x2="0.41333333" y2="-0.67333335"/> <atom id="GDP-atom13" elementType="O" x2="-0.25333333" y2="-0.6666667"/> <atom id="GDP-atom14" elementType="O" x2="0.85333335" y2="-1.0"/> <atom id="GDP-atom15" elementType="O" x2="-0.25333333" y2="-0.12"/> <atom id="GDP-atom16" elementType="H" x2="0.0" y2="0.54333335"/> <atom id="GDP-atom17" elementType="O" x2="0.4" y2="0.85"/> <atom id="GDP-atom18" elementType="H" x2="0.85333335" y2="-0.67333335"/> <atom id="GDP-atom19" elementType="C" x2="0.26666668" y2="-0.5733333"/> <atom id="GDP-atom20" elementType="C" x2="0.4" y2="0.57666665"/> <atom id="GDP-atom21" elementType="O" x2="-0.7266667" y2="-0.6666667"/> <atom id="GDP-atom22" elementType="H" x2="0.26666668" y2="-0.7366667"/> <atom id="GDP-atom23" elementType="P" x2="-0.25333333" y2="-0.39333335"/> <atom id="GDP-atom24" elementType="C" x2="0.85333335" y2="-0.83666664"/> <atom id="GDP-atom25" elementType="O" x2="-1.0" y2="-0.39333335"/> <atom id="GDP-atom26" elementType="O" x2="-0.45" y2="-0.39333335"/> <atom id="GDP-atom27" elementType="C" x2="0.99666667" y2="-0.5733333"/> <atom id="GDP-atom28" elementType="C" x2="0.18" y2="0.2"/> <atom id="GDP-atom29" elementType="C" x2="0.41333333" y2="-0.83666664"/> <atom id="GDP-atom30" elementType="C" x2="0.62" y2="0.2"/> <atom id="GDP-atom31" elementType="O" x2="0.62666667" y2="-0.35666665"/> <atom id="GDP-atom32" elementType="P" x2="-0.7266667" y2="-0.39333335"/> <atom id="GDP-atom33" elementType="O" x2="0.02" y2="-0.39333335"/> </atomArray> <bondArray> <bond id="GDP-bond1" atomRefs="GDP-atom33 GDP-atom6" order="1"/> <bond id="GDP-bond2" atomRefs="GDP-atom32 GDP-atom26" order="1"/> <bond id="GDP-bond3" atomRefs="GDP-atom31 GDP-atom27" order="1"/> <bond id="GDP-bond4" atomRefs="GDP-atom30 GDP-atom4" order="A"/> <bond id="GDP-bond5" atomRefs="GDP-atom30 GDP-atom3" order="A"/> <bond id="GDP-bond6" atomRefs="GDP-atom29 GDP-atom24" order="1"/> <bond id="GDP-bond7" atomRefs="GDP-atom28 GDP-atom5" order="A"/> <bond id="GDP-bond8" atomRefs="GDP-atom27 GDP-atom24" order="1"/> <bond id="GDP-bond9" atomRefs="GDP-atom27 GDP-atom3" order="1"/> <bond id="GDP-bond10" atomRefs="GDP-atom26 GDP-atom23" order="1"/> <bond id="GDP-bond11" atomRefs="GDP-atom25 GDP-atom32" order="2"/> <bond id="GDP-bond12" atomRefs="GDP-atom23 GDP-atom33" order="1"/> <bond id="GDP-bond13" atomRefs="GDP-atom22 GDP-atom19" order="1"/> <bond id="GDP-bond14" atomRefs="GDP-atom21 GDP-atom32" order="1"/> <bond id="GDP-bond15" atomRefs="GDP-atom20 GDP-atom11" order="A"/> <bond id="GDP-bond16" atomRefs="GDP-atom19 GDP-atom29" order="1"/> <bond id="GDP-bond17" atomRefs="GDP-atom19 GDP-atom31" order="1"/> <bond id="GDP-bond18" atomRefs="GDP-atom18 GDP-atom24" order="1"/> <bond id="GDP-bond19" atomRefs="GDP-atom17 GDP-atom20" order="2"/> <bond id="GDP-bond20" atomRefs="GDP-atom16 GDP-atom5" order="1"/> <bond id="GDP-bond21" atomRefs="GDP-atom15 GDP-atom23" order="2"/> <bond id="GDP-bond22" atomRefs="GDP-atom14 GDP-atom24" order="1"/> <bond id="GDP-bond23" atomRefs="GDP-atom13 GDP-atom23" order="1"/> <bond id="GDP-bond24" atomRefs="GDP-atom12 GDP-atom29" order="1"/> <bond id="GDP-bond25" atomRefs="GDP-atom11 GDP-atom30" order="A"/> <bond id="GDP-bond26" atomRefs="GDP-atom10 GDP-atom29" order="1"/> <bond id="GDP-bond27" atomRefs="GDP-atom9 GDP-atom11" order="A"/> <bond id="GDP-bond28" atomRefs="GDP-atom8 GDP-atom32" order="1"/> <bond id="GDP-bond29" atomRefs="GDP-atom7 GDP-atom9" order="A"/> <bond id="GDP-bond30" atomRefs="GDP-atom6 GDP-atom19" order="1"/> <bond id="GDP-bond31" atomRefs="GDP-atom5 GDP-atom20" order="A"/> <bond id="GDP-bond32" atomRefs="GDP-atom4 GDP-atom28" order="A"/> <bond id="GDP-bond33" atomRefs="GDP-atom3 GDP-atom7" order="A"/> <bond id="GDP-bond34" atomRefs="GDP-atom2 GDP-atom27" order="1"/> <bond id="GDP-bond35" atomRefs="GDP-atom1 GDP-atom28" order="1"/> </bondArray> <formula concise="C 10 H 15 N 5 O 11 P 2" formalCharge="-3"/> <float title="molecularWeight" units="g/mol">443.203</float> <string title="smiles">C(OP(O)(=O)OP(O)(=O)O)[CH]1(O[CH]([CH](O)[CH]1O)n2(c3(c(nc2)c(=O)[nH]c(n3)N)))</string> </molecule> </cml> CML ppG guanosine-5'-diphosphate guanosine-diphosphate 443.2030029296875 GDP 1.0 ACTIVATION-ALLOSTERIC INHIBITION-UNKMECH REVERSIBLE 1981 Eur J Biochem 1981;117(3);569-74 PubMed Regulatory properties of phosphofructokinase 2 from Escherichia coli. 6456900 Kotlarz D Buc H fructose-6-phosphate-1-phosphotransferase This enzyme is an isozyme with phosphofructokinase-1. The nucleotide sequences of the genes are not similar.|CITS: [85203917]| 2 Eur J Biochem 1985;149(2);363-73 3158524 Hellinga HW Evans PR PubMed Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase. 1985 6PFK-2-CPX PFK II 6-phosphofructokinase-2 149128 J Biol Chem 1978;253(12);4350-5 Babul J PubMed 1978 Phosphofructokinases from Escherichia coli. Purification and characterization of the nonallosteric isozyme. fructose-6-p-1-kinase Pfk-2 is somewhat sensitive to inhibition by fructose-1,6-diphosphate and ATP. Pfk-2,unlike pfk-1, does not show cooperative interaction with fructose-6-phosphate, inhibition by PEP or activation by ADP. |CITS:[84262485]| MgATP is an inhibitor of pfk-2 and it provokes the tetramerization of the dimeric native enzyme.|CITS: [85289307],[88292964]| Its normal function is not known and in strains with pfk-1, pfkB may be deleted without apparent effect. |CITS: [83294514]| However in the absence of pfk-1, slow growth on sugars depends on pfk-2. Its loss causes complete inability to grow. |CITS: [84262485]| The distribution of the two phosphofructokinases is variable among enterobacteria and also among E.coli strains |CITS: [82027179]| NP_417400 RefSeq 1DOS PDB <cml> <molecule id="CIT" title="citrate" dictRef="dictCIT"> <atomArray> <atom id="CIT-atom1" elementType="O" x2="-0.62098" y2="0.17428"/> <atom id="CIT-atom2" elementType="O" x2="0.6176" y2="0.20135"/> <atom id="CIT-atom3" elementType="O" x2="-1.0" y2="-0.20474"/> <atom id="CIT-atom4" elementType="C" x2="-0.022" y2="-0.45516"/> <atom id="CIT-atom5" elementType="C" x2="-0.62098" y2="-0.20474"/> <atom id="CIT-atom6" elementType="C" x2="-0.022" y2="-0.7665"/> <atom id="CIT-atom7" elementType="C" x2="-0.47885" y2="-0.45516"/> <atom id="CIT-atom8" elementType="O" x2="-0.022" y2="-0.07614"/> <atom id="CIT-atom9" elementType="O" x2="0.27919" y2="-1.0"/> <atom id="CIT-atom10" elementType="C" x2="0.36379" y2="-0.45516"/> <atom id="CIT-atom11" elementType="O" x2="0.99662" y2="-0.17766"/> <atom id="CIT-atom12" elementType="O" x2="-0.3198" y2="-1.0"/> <atom id="CIT-atom13" elementType="C" x2="0.6176" y2="-0.17766"/> </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 8 O 7" formalCharge="0"/> <float title="molecularWeight" units="g/mol">192.125</float> <string title="smiles">C(=O)(O)CC(C(O)=O)(O)CC(O)=O</string> </molecule> </cml> CML citrate citric acid citr cit 192.125 CAS 77-92-9 2-hydroxy-1,2,3-propanetricarboxylic acid 1TMH PDB Tpi b3919 PIR triose phosphate isomerase monomer PDB 1TRE MRHPLVMGNWKLNGSRHMVHELVSNLRKELAGVAGCAVAIAPPEMYIDMAKREAEGSHIMLGAQNVDLNLSGAFTGETSAAMLKDIGAQYIIIGHSERRTYHKESDELIAKKFAVLKEQGLTPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKVDANIAEQVIIQYGGSVNASNAAELFAQPDIDGALVGGASLKADAFAVIVKAAEAAKQA P04790 SWISS-PROT NP_418354 RefSeq P04790 SWISS-MODEL TPIA-MONOMER EcoO157Cyc Ortholog TpiA B3919 2 Purification and characterization of two fructose diphosphate aldolases from Escherichia coli (Crookes' strain). PubMed 4198624 Perham RN 1973 Stribling D Biochem J 1973;131(4);833-41 D-glucose-6-P &alpha;-D-glucose-6-phosphate 260.1369934082031 &alpha;-D-glucose-6-P D-glucose-6-phosphate glucose-6-P <cml> <molecule id="GLC-6-P" title="glucose-6-phosphate" dictRef="dictGLC-6-P"> <atomArray> <atom id="GLC-6-P-atom1" elementType="H" x2="-1.0" y2="-0.13312"/> <atom id="GLC-6-P-atom2" elementType="C" x2="-0.68182" y2="0.32792"/> <atom id="GLC-6-P-atom3" elementType="O" x2="-0.37338" y2="0.62013"/> <atom id="GLC-6-P-atom4" elementType="O" x2="0.00974" y2="0.24351"/> <atom id="GLC-6-P-atom5" elementType="C" x2="-0.06494" y2="-0.77273"/> <atom id="GLC-6-P-atom6" elementType="P" x2="0.00974" y2="0.62013"/> <atom id="GLC-6-P-atom7" elementType="C" x2="0.26299" y2="-0.36039"/> <atom id="GLC-6-P-atom8" elementType="C" x2="-0.68182" y2="-0.77273"/> <atom id="GLC-6-P-atom9" elementType="O" x2="0.00974" y2="0.99675"/> <atom id="GLC-6-P-atom10" elementType="O" x2="-0.68182" y2="-0.54545"/> <atom id="GLC-6-P-atom11" elementType="H" x2="0.26299" y2="-0.13312"/> <atom id="GLC-6-P-atom12" elementType="C" x2="-1.0" y2="-0.36039"/> <atom id="GLC-6-P-atom13" elementType="H" x2="-0.06494" y2="-0.54545"/> <atom id="GLC-6-P-atom14" elementType="O" x2="-0.06494" y2="0.06494"/> <atom id="GLC-6-P-atom15" elementType="O" x2="0.38636" y2="0.62013"/> <atom id="GLC-6-P-atom16" elementType="O" x2="-0.06494" y2="-1.0"/> <atom id="GLC-6-P-atom17" elementType="C" x2="-0.68182" y2="0.06494"/> <atom id="GLC-6-P-atom18" elementType="O" x2="0.26299" y2="-0.58766"/> <atom id="GLC-6-P-atom19" elementType="H" x2="-0.68182" y2="-1.0"/> <atom id="GLC-6-P-atom20" elementType="O" x2="-1.0" y2="-0.58766"/> <atom id="GLC-6-P-atom21" elementType="H" x2="-0.68182" y2="-0.16234"/> </atomArray> <bondArray> <bond id="GLC-6-P-bond1" atomRefs="GLC-6-P-atom21 GLC-6-P-atom17" order="1"/> <bond id="GLC-6-P-bond2" atomRefs="GLC-6-P-atom20 GLC-6-P-atom12" order="1"/> <bond id="GLC-6-P-bond3" atomRefs="GLC-6-P-atom19 GLC-6-P-atom8" order="1"/> <bond id="GLC-6-P-bond4" atomRefs="GLC-6-P-atom18 GLC-6-P-atom7" order="1"/> <bond id="GLC-6-P-bond5" atomRefs="GLC-6-P-atom17 GLC-6-P-atom12" order="1"/> <bond id="GLC-6-P-bond6" atomRefs="GLC-6-P-atom16 GLC-6-P-atom5" order="1"/> <bond id="GLC-6-P-bond7" atomRefs="GLC-6-P-atom15 GLC-6-P-atom6" order="1"/> <bond id="GLC-6-P-bond8" atomRefs="GLC-6-P-atom14 GLC-6-P-atom17" order="1"/> <bond id="GLC-6-P-bond9" atomRefs="GLC-6-P-atom14 GLC-6-P-atom7" order="1"/> <bond id="GLC-6-P-bond10" atomRefs="GLC-6-P-atom13 GLC-6-P-atom5" order="1"/> <bond id="GLC-6-P-bond11" atomRefs="GLC-6-P-atom12 GLC-6-P-atom8" order="1"/> <bond id="GLC-6-P-bond12" atomRefs="GLC-6-P-atom11 GLC-6-P-atom7" order="1"/> <bond id="GLC-6-P-bond13" atomRefs="GLC-6-P-atom10 GLC-6-P-atom8" order="1"/> <bond id="GLC-6-P-bond14" atomRefs="GLC-6-P-atom9 GLC-6-P-atom6" order="2"/> <bond id="GLC-6-P-bond15" atomRefs="GLC-6-P-atom8 GLC-6-P-atom5" order="1"/> <bond id="GLC-6-P-bond16" atomRefs="GLC-6-P-atom7 GLC-6-P-atom5" order="1"/> <bond id="GLC-6-P-bond17" atomRefs="GLC-6-P-atom6 GLC-6-P-atom3" order="1"/> <bond id="GLC-6-P-bond18" atomRefs="GLC-6-P-atom4 GLC-6-P-atom6" order="1"/> <bond id="GLC-6-P-bond19" atomRefs="GLC-6-P-atom3 GLC-6-P-atom2" order="1"/> <bond id="GLC-6-P-bond20" atomRefs="GLC-6-P-atom2 GLC-6-P-atom17" order="1"/> <bond id="GLC-6-P-bond21" atomRefs="GLC-6-P-atom1 GLC-6-P-atom12" order="1"/> </bondArray> <formula concise="C 6 H 13 O 9 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">260.137</float> <string title="smiles">C(OP(=O)(O)O)[CH]1([CH](O)[CH](O)[CH](O)[CH](O)O1)</string> </molecule> </cml> CML glucose-6-phosphate 1 PHOSPHOGLUCOISOMERASE OXOISOMERASE 5.3.1.9 PHOSPHOGLUCOSE ISOMERASE PHOSPHOSACCHAROMUTASE PHOSPHOHEXOMUTASE PHOSPHOHEXOISOMERASE 0.4 HEXOSEPHOSPHATE ISOMERASE PHOSPHOHEXOSE ISOMERASE PGLUCISOM-RXN TPI Ortholog EcoO157Cyc FBA-MONOMER PDB 1ZEN CML <cml> <molecule id="GLYCEROL-3P" title="glycerol-3-phosphate" dictRef="dictGLYCEROL-3P"> <atomArray> <atom id="GLYCEROL-3P-atom1" elementType="O" x2="-0.06931" y2="0.43564"/> <atom id="GLYCEROL-3P-atom2" elementType="O" x2="-1.0" y2="-0.29703"/> <atom id="GLYCEROL-3P-atom3" elementType="P" x2="0.63036" y2="-0.63036"/> <atom id="GLYCEROL-3P-atom4" elementType="O" x2="0.25413" y2="-0.88779"/> <atom id="GLYCEROL-3P-atom5" elementType="C" x2="-0.07261" y2="-0.26073"/> <atom id="GLYCEROL-3P-atom6" elementType="O" x2="0.36964" y2="-0.26073"/> <atom id="GLYCEROL-3P-atom7" elementType="C" x2="-0.72277" y2="0.06271"/> <atom id="GLYCEROL-3P-atom8" elementType="C" x2="-0.33003" y2="0.06271"/> <atom id="GLYCEROL-3P-atom9" elementType="O" x2="0.9967" y2="-0.35974"/> <atom id="GLYCEROL-3P-atom10" elementType="O" x2="0.90099" y2="-1.0"/> </atomArray> <bondArray> <bond id="GLYCEROL-3P-bond1" atomRefs="GLYCEROL-3P-atom10 GLYCEROL-3P-atom3" order="1"/> <bond id="GLYCEROL-3P-bond2" atomRefs="GLYCEROL-3P-atom9 GLYCEROL-3P-atom3" order="2"/> <bond id="GLYCEROL-3P-bond3" atomRefs="GLYCEROL-3P-atom8 GLYCEROL-3P-atom5" order="1"/> <bond id="GLYCEROL-3P-bond4" atomRefs="GLYCEROL-3P-atom7 GLYCEROL-3P-atom8" order="1"/> <bond id="GLYCEROL-3P-bond5" atomRefs="GLYCEROL-3P-atom6 GLYCEROL-3P-atom3" order="1"/> <bond id="GLYCEROL-3P-bond6" atomRefs="GLYCEROL-3P-atom5 GLYCEROL-3P-atom6" order="1"/> <bond id="GLYCEROL-3P-bond7" atomRefs="GLYCEROL-3P-atom4 GLYCEROL-3P-atom3" order="1"/> <bond id="GLYCEROL-3P-bond8" atomRefs="GLYCEROL-3P-atom2 GLYCEROL-3P-atom7" order="1"/> <bond id="GLYCEROL-3P-bond9" atomRefs="GLYCEROL-3P-atom1 GLYCEROL-3P-atom8" order="1"/> </bondArray> <formula concise="C 3 H 9 O 6 P 1" formalCharge="0"/> <float title="molecularWeight" units="g/mol">172.074</float> <string title="smiles">C(C(O)CO)OP(=O)(O)O</string> </molecule> </cml> &alpha;-glycerophosphate glycerol-3-P glycerol-3-phosphate D-glycerol-3-phosphate 172.07400512695312 CAS 57-03-4 sn-glycerol-3-phosphate P11537 SWISS-PROT PIR b4025 Baldwin SA Perham RN Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli. Alefounder PR PubMed Short NJ Biochem J 1989;257(2);529-34 1989 2649077 In relation to the Class I enzymes (primarily studied and found in eukaryotes) comparatively little is known about the class II enzymes. The Class II aldolases of Sacc. cer. and E. coli are the best characterized.|CITS: [89193446]| It resembles the typical class II aldolase from yeast in size and amino acid composition. This is a strong suggestion that they are related. |CITS:[78165651]| These less well studied aldolases are found both in the eukaryotic green algae and fungi, and in the prokaryotic blue-green algae and bacteria. |CITS:[78165651]| The gene pgk, encoding the enzyme phosphoglycerate kinase, was carried on plasmid pLC33-5 of the collection of Clarke and Carbon. It was also noted that E.coli cells tansformed with this plasmid exhibited raised levels of Class II fructose 1,6 bisphosphate aldolase activity, suggesting that the same plasmid might also carry the structural gene (fba) for this enzyme. |CITS: [89193446]| Biochem J 1978;169(3);633-41 1978 Stribling D Baldwin SA PubMed Perham RN Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain). 417719 2 Fda The amino acid sequence of the E.coli Class II fructose-1,6-bisphosphate aldolase inferred from the DNA sequence of the fda gene is the first primary structure of a Class II aldolase to be established. There is no immediately apparent sequence homology with any of the Class I fructose-1,6-bisphosphate aldolases which have been widely studied. |CITS:[89193446]| An fda mutant exhibits a heat-sensitive defect in rRNA transcription that is elicited via altered abundance of ppGpp and of initiating NTPs |CITS: [14526031]|. Fda has similarity to an <i>Edwardsiella ictaluri</i> protein that provokes an immune response in catfish |CITS: [12542086]|. SWISS-PROT P11604 MSKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELGCTGGEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVHGVYKPGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL FbaA fructose bisphosphate aldolase monomer b2925 PIR Ald Fba B2925 FRUCBISALD-CLASSII PubMed Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli. Mol Gen Genet 1989;217(1);126-31 Gottlieb LD Froman BE Tait RC 2549364 1989 FRUCBISALD-CLASSI 10 Z3260-MONOMER EcoO157Cyc Ortholog RefSeq NP_416600 fructose bisphosphate aldolase monomer SWISS-PROT P71295 PIR b2097 MIARKRRARTIHSRYPIGIYGSIVMTDIAQLLGKDADNLLQHRCMTIPSDQLYLPGHDYVDRVMIDNNRPPAVLRNMQTLYNTGRLAGTGYLSILPVDQGVEHSAGASFAANPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQTLYASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKDGVDYHVSADLTGQANHLAATIGADIVKQKMAENNGGYKAINYGYTDDRVYSKLTSENPIDLVRYQLANCYMGRAGLINSGGAAGGETDLSDAVRTAVINKRAGGMGLILGRKAFKKSMADGVKLINAVQDVYLDSKITIA DhnA FbaB B2097 The typical class I aldolases of plants and animals have been throroughly studied |CITS: [78165651]| Fructose-1,6-bisphosphate aldolases can be divided into two classes on the basis of their catalytic and structural properties. |CITS: [78165651]| Class I fructose 1,6 bisphosphate aldolases were once thought to be confined to eukaryotic organisms but have since been detected in several bacterial species. |CITS: [78165652]| The occurence of such an aldolase in bacteria was unexpected in light of the phylogenetic distribution of aldolases. |CITS: [73229139]| The enzymes of eukaryotes generally fall into Class I and are tetramers of identical polypeptide chains. |CITS: [89193446]| In earlier studies |CITS: [73229139]| it was thought that the class I E. coli aldolase was typical in that it was tetrameric with a mol. wt. of approx. 140K. In 1978 new purification techniques were used.The true aldolase 1 activity could be measured by using Fru-1,6-P<SUB>2</SUB> that had been purified by chromatography on DEAE-cellulose to remove the fructose-6-phosphate. Using these methods the enzyme appeared to be larger than was previously supposed and may be a decamer with a mol. wt. of approx. 340,000. The size of aldolase 1 and the effect of cross-linking reagents on it, indicate that its structure must differ significantly from that of the typical tetrameric class-I enzymes from eukaryotes. |CITS: [78165652] [73229139]| PGI-MONOMER Ortholog EcoO157Cyc MKNINPTQTAAWQALQKHFDEMKDVTIADLFAKDGDRFSKFSATFDDQMLVDYSKNRITEETLAKLQDLAKECDLAGAIKSMFSGEKINRTENRAVLHVALRNRSNTPILVDGKDVMPEVNAVLEKMKTFSEAIISGEWKGYTGKAITDVVNIGIGGSDLGPYMVTEALRPYKNHLNMHFVSNVDGTHIAEVLKKVNPETTLFLVASKTFTTQETMTNAHSARDWFLKAAGDEKHVAKHFAALSTNAKAVGEFGIDTANMFEFWDWVGGRYSLWSAIGLSIVLSIGFDNFVELLSGAHAMDKHFSTTPAEKNLPVLLALIGIWYNNFFGAETEAILPYDQYMHRFAAYFQQGNMESNGKYVDRNGNVVDYQTGPIIWGEPGTNGQHAFYQLIHQGTKMVPCDFIAPAITHNPLSDHHQKLLSNFFAQTEALAFGKSREVVEQEYRDQGKDPATLDYVVPFKVFEGNRPTNSILLREITPFSLGALIALYEHKIFTQGVILNIFTFDQWGVELGKQLANRILPELKDDKEISSHDSSTNGLINRYKAWRG PGLUCISOM B4025 Pgi phosphoglucose isomerase is found primarily in the cytoplasm RefSeq NP_418449 When E. coli K-12 is grown on C-3 carbon sources both classes of aldolase are present. However the Class I enzyme is present only under these conditions. Therefore it is likely that the Class I enzyme is involved in gluconeogenesis and the class II enzyme in glycolysis. |CITS: [81000551]| The class I enzymes function by imine formation between the substrate and a catalytically essential lysine residue in the active site, which acts to stabilize the intermediate carbanion. |CITS:[89193446]| They form a Schiff base betwen the E-amino group of a specific lysine residue in the active site and the carbonyl group of the substrate. This imine may be reduced by borohydride which therefore irreversibly inhibits class 1 aldolases in the presence of substrate. |CITS:[73229139]| The enzyme's activity was unaffected by EDTA, but it was inhibited by borohydride reduction in the presence of Fru-1,6-P2 or dihydroxyacetone phosphate. Like mammalian aldolases, it cleaved fructose 1-phosphate, albeit slowly and had a low Km for Fru-1,6-P2. Its fructose 1,6 bisphosphate cleavage activity was greatly enhanced by citrate, PEP, 2-oxoglutarate and sn-glycerol 3-phosphate. Aldolase I is very efficient at Fru-1,6-P2 cleavage when fully activated. Only a limited range of metabolites has been tested as possible activators. In contrast, its fructose 1-phosphate cleavage activity was unaffected by these compounds. The enhancement exhibited a strong dependence on pH. These novel kinetic properties do not seem to be shared by any other fructose 1,6 bisphosphate aldolase. In view of its unusual properties, it is unlikely that aldolase I from E.coli is closely related to the class-1 aldolases that have been detected in several other prokaryotes, or to the typical class I enzymes from eukaryote. |CITS: [78165652]| Howlett GJ 9531482 1998 PubMed Biochem J 1998;331 ( Pt 2);437-45 Berry A Thomson GJ Ashcroft AE The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase. fructose bisphosphate aldolase class I REVERSIBLE F16ALDOLASE-RXN FRUCTOSE-1,6-BISPHOSPHATE TRIOSEPHOSPHATE-LYASE Dihydroxyacetone phosphate is also called glycerone phosphate. Of the total aldolase activity in cell-free extracts of E.coli grown on pyruvate and lactate, approx. 60 % was accounted for by aldolase 1. On the other hand, E.coli grown on glucose showed no aldolase 1 activity but had an increased aldolase 2 activity. |CITS: [73229139]| During growth with CO2 as a carbon source, only class I aldolase is produced but when acetate replaces CO2 the class II aldolase is made. Similarly, in E.coli the putative class I aldolase is only synthesized during growth on C3 compounds and not on glucose, implying that a class I aldolase is preferred for gluconeogenesis |CITS:[73229139]| 5.7 4.1.2.13 ALDOLASE phosphotriose isomerase triosephosphate isomerase The amino acid sequence around the active site is perfectly conserved in all known triose phosphate isomerases and can be used as a signature pattern for this type of enzyme.|CITS: [Prosite]| TIM PHOSPHOTRIOSE ISOMERASE 5.3.1.1 TRIOSEPHOSPHATE MUTASE triose phosphate isomerization triosephosphate mutase triose phosphate isomerase REVERSIBLE fructose bisphosphate aldolase class II REVERSIBLE Class II enzymes utilize a divalent metal ion to act as the electron sink at the active site in what appears to be an otherwise similar catalytic mechanism to Class I. |CITS: [89193446]| The metal ion in the active site varies, but several metals including zinc, cobalt, iron, nickel and manganese can form an active metallo-protein complex |CITS: [73229139]| In Crookes strain of E. coli it was found that the kinetic behavior is not typical of a class-II aldolase; the enzyme has no requirement for thiol compounds either for stability or activity, added K+ ions have no effect, and the high pH optimum of 9 is unusual for a class II enzyme. |CITS: [78165651]| Aldolase II is relatively insensitive to compounds that react with thiol groups.|CITS: [78165651]| It is strongly inhibited by metal-chelating agents and is reactivated by bivalent metal ions.|CITS: [73229139]| When E. coli K-12 is grown on C-3 carbon sources both classes of aldolase are present. However the Class I enzyme is present only under these conditions. Therefore the Class I enzyme is most likely involved in gluconeogenesis and the Class II enzyme with glycolysis. |CITS: [81000551]| fructose-1,6-bisphosphate triosephosphate lyase fructose-1,6-bisphosphate aldolase INHIBITION-UNKMECH 1.0 EDTA INHIBITION-UNKMECH 1.0 BOROHYDRIDE This pathway is freely available to all users and may be redistributed in whole or in part provided proper source attribution is made. See http://biocyc.org/open-reg.shtml for more information. ACTIVATION-ALLOSTERIC ACTIVATION-UNKMECH ACTIVATION-UNKMECH 1.0 INHIBITION-UNKMECH ACTIVATION-UNKMECH 1.0 INHIBITION-ALLOSTERIC INHIBITION-UNKMECH ACTIVATION-UNKMECH Embden-Meyerhof pathway glycolysis I EcoCyc Database (http://ecocyc.org) Pyruvate from glycolysis proceeds to the pyruvate dehydrogenase multienzyme complex, and the acetyl CoA produced then proceeds on to the superpathway of glyoxylate bypass and TCA. REVERSIBLE glucose-6-phosphate isomerase 2-deoxyglucose-6-p is a known inhibitor in mammalian systems. E.coli cells with mutated pgi gene apparently utilize glucose primarily by the pentose phosphate pathway and to a lesser extent by the Entner-Duodoroff pathway. |CITS:[89364675]| D-glucose-6-phosphate-ketol-isomerase phosphoglucose isomerase Intracellular pH effect upon phosphoglucose isomerase in Escherichia coli Klungsoyr L BBA 1964;92:378-387 Endresen A glucose degradation