Homocitrate synthase

In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction

α-Ketoglutaric acid

+ acetyl-CoA

 

 

H₂O

 

H₂O

 

 

(-)-Homoisocitric acid

+ Coenzyme A

 

homocitrate synthase
Homocitrate synthase homodimer, Schizosaccharomyces pombe
Identifiers
EC no.	2.3.3.14
CAS no.	9075-60-9
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

The three substrates of this enzyme are α-ketoglutaric acid, acetyl-CoA, and water. Its products are (-)-homoisocitric acid and coenzyme A.^[1][2][3][4]

This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:2-oxoglutarate C-acetyltransferase (thioester-hydrolysing, carboxymethyl forming). Other names in common use include 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase, (CoA-acetylating), acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase, and homocitrate synthetase. This enzyme participates in lysine biosynthesis and pyruvate metabolism.