Phosphopyruvate hydratase
| phosphopyruvate hydratase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 4.2.1.11 | ||||||
| CAS number | 9014-08-8 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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In enzymology, a phosphopyruvate hydratase (EC 4.2.1.11) is an enzyme that catalyzes the chemical reaction
- 2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Hence, this enzyme has one substrate, 2-phospho-D-glycerate, and two products, phosphoenolpyruvate and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming). Other names in common use include enolase, 2-phosphoglycerate dehydratase, 14-3-2-protein, nervous-system specific enolase, phosphoenolpyruvate hydratase, 2-phosphoglycerate dehydratase, 2-phosphoglyceric dehydratase, 2-phosphoglycerate enolase, gamma-enolase, and 2-phospho-D-glycerate hydro-lyase. This enzyme participates in glycolysis/gluconeogenesis. At least one compound, Phosphonoacetohydroxamate is known to inhibit this enzyme. The human gene that makes this enzyme is ENO2.
Structural studies
As of late 2007, 27 structures have been solved for this class of enzymes, with PDB accession codes 1E9I, 1EBG, 1EBH, 1ELS, 1IYX, 1L8P, 1NEL, 1OEP, 1ONE, 1P43, 1P48, 1PDY, 1PDZ, 1TE6, 1W6T, 2AKM, 2AKZ, 2AL1, 2AL2, 2FYM, 2ONE, 2PA6, 3ENL, 4ENL, 5ENL, 6ENL, and 7ENL.
References
- HOLT A, WOLD F (1961). "The isolation and characterization of rabbit muscle enolase". J. Biol. Chem. 236: 3227–31. PMID 13908561.
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 471-494.
- WESTHEAD EW, MCLAIN G (1964). "A PURIFICATION OF BREWERS' AND BAKERS' YEAST ENOLASE YIELDING A SINGLE ACTIVE COMPONENT". J. Biol. Chem. 239: 2464–8. PMID 14235523.