Homocitrate synthase

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

acetyl-CoA + H₂O + 2-oxoglutarate ${\displaystyle \rightleftharpoons }$ (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA

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 3 substrates of this enzyme are acetyl-CoA, H₂O, and 2-oxoglutarate, whereas its two products are (R)-2-hydroxybutane-1,2,4-tricarboxylate and CoA.

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.