Enolase

phosphopyruvate hydratase
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
Search PMC articles PubMed articles NCBI proteins

Enolase, N-terminal domain
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
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Enolase
Crystal structure of dimeric beta human enolase ENO3.[2]
Identifiers
Symbol	Enolase
Pfam	PF00113
InterPro	IPR000941
PROSITE	PDOC00148
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB PDB: 1e9i​ PDB: 1ebg​ PDB: 1ebh​ PDB: 1els​ PDB: 1iyx​ PDB: 1l8p​ PDB: 1nel​ PDB: 1oep​ PDB: 1one​ PDB: 1p43​

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:

2-phospho-D-glycerate ${\displaystyle \rightleftharpoons }$ phosphoenolpyruvate + H₂O

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.