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Escherichia coli K-12 substr. MG1655 Compound: phosphoenolpyruvate

Synonyms: P-enol-pyr, P-enol-pyruvate, P-enol-pyruvate, P-enol-pyr, PEP

Component of: IclR-PEP

Chemical Formula: C3H2O6P

Molecular Weight: 165.02 Daltons

Monoisotopic Molecular Weight: 167.9823744031 Daltons

phospho<i>enol</i>pyruvate compound structure

SMILES: C=C(OP([O-])([O-])=O)C([O-])=O

InChI: InChI=1S/C3H5O6P/c1-2(3(4)5)9-10(6,7)8/h1H2,(H,4,5)(H2,6,7,8)/p-3


Unification Links: CAS:73-89-2, CAS:138-08-9, ChEBI:58702, ChemSpider:2907208, HMDB:HMDB00263, IAF1260:33756, KEGG:C00074, PubChem:3674425

Standard Gibbs Free Energy of Formation (ΔfG in kcal/mol): -311.57

Reactions known to consume the compound:

3-dehydroquinate biosynthesis I :
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O → 3-deoxy-D-arabino-heptulosonate-7-phosphate + phosphate

CMP-3-deoxy-D-manno-octulosonate biosynthesis :
D-arabinofuranose 5-phosphate + phosphoenolpyruvate + H2O → 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate

glycerol degradation V :
dihydroxyacetone + phosphoenolpyruvate → glycerone phosphate + pyruvate

glycolysis I (from glucose 6-phosphate) , glycolysis II (from fructose 6-phosphate) , mixed acid fermentation :
pyruvate + ATP ← ADP + phosphoenolpyruvate + H+

UDP-N-acetylmuramoyl-pentapeptide biosynthesis I (meso-diaminopimelate containing) :
UDP-N-acetyl-α-D-glucosamine + phosphoenolpyruvate → UDP-N-acetyl-α-D-glucosamine-enolpyruvate + phosphate

Not in pathways:
phosphoenolpyruvate + a [PTS enzyme I]-L-histidine → pyruvate + a [PTS enzyme I]-Nπ-phospho-L-histidine
phosphoenolpyruvate[periplasm] + H2O[periplasm] → pyruvate[periplasm] + phosphate[periplasm]

Reactions known to produce the compound:

gluconeogenesis I :
pyruvate + ATP + H2O → phosphoenolpyruvate + AMP + phosphate + 2 H+
oxaloacetate + ATP → CO2 + phosphoenolpyruvate + ADP

glycolysis I (from glucose 6-phosphate) , glycolysis II (from fructose 6-phosphate) :
pyruvate + ATP + H2O → phosphoenolpyruvate + AMP + phosphate + 2 H+

Reactions known to both consume and produce the compound:

chorismate biosynthesis from 3-dehydroquinate :
shikimate 3-phosphate + phosphoenolpyruvate ↔ 5-enolpyruvyl-shikimate 3-phosphate + phosphate

gluconeogenesis I , glycolysis I (from glucose 6-phosphate) , glycolysis II (from fructose 6-phosphate) :
2-phospho-D-glycerate ↔ phosphoenolpyruvate + H2O

mixed acid fermentation :
oxaloacetate + phosphate ↔ phosphoenolpyruvate + hydrogen carbonate

In Reactions of unknown directionality:

Not in pathways:
phosphoenolpyruvate + PtsI = pyruvate + PtsI-Phis189
phosphoenolpyruvate + PtsP = pyruvate + PtsP-phosphorylated
IclR + phosphoenolpyruvate = IclR-PEP

Enzymes activated by phosphoenolpyruvate, sorted by the type of activation, are:

Activator (Mechanism unknown) of: 3-phosphoshikimate-1-carboxyvinyltransferase [Gruys92], phosphate acetyltransferase [CamposBermudez10], fructose-1,6-bisphosphatase [Hines06], isocitrate dehydrogenase phosphatase [Nimmo84], fructose bisphosphate aldolase [Baldwin78], fructose 1,6-bisphosphatase [Donahue00]

Enzymes inhibited by phosphoenolpyruvate, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: glycerol-3-phosphate dehydrogenase, aerobic [Schryvers78], phosphoglucose isomerase [Ogawa07], glucokinase [Ogawa07], isocitrate lyase Inhibitor (Allosteric) of: isocitrate dehydrogenase [Ogawa07a], 6-phosphofructokinase [Fraenkel73, Blangy68] Inhibitor (Mechanism unknown) of: phosphate acetyltransferase [CamposBermudez10], thiamine phosphate synthase [Kayama73, Kawasaki79], fructose-1,6-bisphosphatase [Babul83], phosphoenolpyruvate synthetase [Cooper69a, Chulavatnatol73], isocitrate lyase, isocitrate dehydrogenase kinase [Nimmo84], phosphoenolpyruvate carboxykinase (ATP) [Krebs80], methylglyoxal synthase [Hopper71, Comment 1], glutamine synthetase adenylyltransferase [Ebner70a, Comment 2]

This compound has been characterized as an alternative substrate of the following enzymes: phosphoglycolate phosphatase, alkaline phosphatase, 6-phosphogluconate phosphatase

In Growth Media: PMA phosphorus source test + phosphoenolpyruvate


Babul83: Babul J, Guixe V (1983). "Fructose bisphosphatase from Escherichia coli. Purification and characterization." Arch Biochem Biophys 1983;225(2);944-9. PMID: 6312898

Baldwin78: Baldwin SA, Perham RN (1978). "Novel kinetic and structural properties of the class-I D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)." Biochem J 1978;169(3);643-52. PMID: 348198

Blangy68: Blangy D, Buc H, Monod J (1968). "Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli." J Mol Biol 31(1);13-35. PMID: 4229913

CamposBermudez10: Campos-Bermudez VA, Bologna FP, Andreo CS, Drincovich MF (2010). "Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation." FEBS J 277(8);1957-66. PMID: 20236319

Chulavatnatol73: Chulavatnatol M, Atkinson DE (1973). "Phosphoenolpyruvate synthetase from Escherichia coli. Effects of adenylate energy charge and modifier concentrations." J Biol Chem 248(8);2712-5. PMID: 4572511

Cooper69a: Cooper RA, Kornberg HL "Phosphoenolpyruvate Synthetase." Methods Enzymol. 1969;13:309-314.

Donahue00: Donahue JL, Bownas JL, Niehaus WG, Larson TJ (2000). "Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli." J Bacteriol 2000;182(19);5624-7. PMID: 10986273

Ebner70a: Ebner E, Wolf D, Gancedo C, Elsasser S, Holzer H (1970). "ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties." Eur J Biochem 1970;14(3);535-44. PMID: 4920894

Fraenkel73: Fraenkel DG, Kotlarz D, Buc H (1973). "Two fructose 6-phosphate kinase activities in Escherichia coli." J Biol Chem 248(13);4865-6. PMID: 4268865

Gruys92: Gruys KJ, Walker MC, Sikorski JA (1992). "Substrate synergism and the steady-state kinetic reaction mechanism for EPSP synthase from Escherichia coli." Biochemistry 31(24);5534-44. PMID: 1344882

Hines06: Hines JK, Fromm HJ, Honzatko RB (2006). "Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase." J Biol Chem 281(27);18386-93. PMID: 16670087

Hopper71: Hopper DJ, Cooper RA (1971). "The regulation of Escherichia coli methylglyoxal synthase; a new control site in glycolysis?." FEBS Lett 13(4);213-216. PMID: 11945670

Hopper72: Hopper DJ, Cooper RA (1972). "The purification and properties of Escherichia coli methylglyoxal synthase." Biochem J 1972;128(2);321-9. PMID: 4563643

Kawasaki79: Kawasaki T (1979). "Thiamine phosphate pyrophosphorylase." Methods Enzymol 1979;62;69-73. PMID: 374983

Kayama73: Kayama Y, Kawasaki T (1973). "Purification and properties of thiaminephosphate pyrophosphorylase of Escherichia coli." Arch Biochem Biophys 1973;158(1);242-8. PMID: 4580841

Krebs80: Krebs A, Bridger WA (1980). "The kinetic properties of phosphoenolpyruvate carboxykinase of Escherichia coli." Can J Biochem 1980;58(4);309-18. PMID: 6991069

Nimmo84: Nimmo GA, Nimmo HG (1984). "The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli ML308 and the roles of these activities in the control of isocitrate dehydrogenase." Eur J Biochem 1984;141(2);409-14. PMID: 6329757

Ogawa07: Ogawa T, Mori H, Tomita M, Yoshino M (2007). "Inhibitory effect of phosphoenolpyruvate on glycolytic enzymes in Escherichia coli." Res Microbiol 158(2);159-63. PMID: 17307338

Ogawa07a: Ogawa T, Murakami K, Mori H, Ishii N, Tomita M, Yoshin M (2007). "Role of phosphoenolpyruvate in the NADP-isocitrate dehydrogenase and isocitrate lyase reaction in Escherichia coli." J Bacteriol 189(3);1176-8. PMID: 17142397

Schryvers78: Schryvers A, Lohmeier E, Weiner JH (1978). "Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli." J Biol Chem 253(3);783-8. PMID: 340460

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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