phosphopyruvate hydratase | |||||||||
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![]() Yeast enolase dimer.[1] | |||||||||
Identifiers | |||||||||
EC no. | 4.2.1.11 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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Enolase, N-terminal domain | |||||||||
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![]() x-ray structure and catalytic mechanism of lobster enolase | |||||||||
Identifiers | |||||||||
Symbol | Enolase_N | ||||||||
Pfam | PF03952 | ||||||||
Pfam clan | CL0227 | ||||||||
InterPro | IPR020811 | ||||||||
PROSITE | PDOC00148 | ||||||||
SCOP2 | 1els / SCOPe / SUPFAM | ||||||||
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Enolase | |||||||||||
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Identifiers | |||||||||||
Symbol | Enolase | ||||||||||
Pfam | PF00113 | ||||||||||
InterPro | IPR000941 | ||||||||||
PROSITE | PDOC00148 | ||||||||||
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Phosphopyruvate hydratase, usually known as enolase, is a metalloenzyme (EC 4.2.1.11) that catalyses the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. The chemical reaction is:
Phosphopyruvate hydratase belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme is 2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming).
The reaction is reversible, depending on environmental concentrations of substrates.[3] The optimum pH for the human enzyme is 6.5.[4] Enolase is present in all tissues and organisms capable of glycolysis or fermentation. The enzyme was discovered by Lohmann and Meyerhof in 1934,[5] and has since been isolated from a variety of sources including human muscle and erythrocytes.[4] In humans, deficiency of ENO1 is linked to hereditary haemolytic anemia, while ENO3 deficiency is linked to glycogen storage disease type XIII.