Acetyl-CoA C-acetyltransferase

acetyl-CoA C-acetyltransferase
Crystallographic structure of the tetrameric acetoacetyl-CoA thiolase (EC:2.3.1.9) from the Gram-negative bacterium Z. ramigera.[1]
Identifiers
EC number	2.3.1.9
CAS number	9027-46-7
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, an acetyl-CoA C-acetyltransferase (EC 2.3.1.9) is an enzyme that catalyzes the chemical reaction

2 acetyl-CoA $\rightleftharpoons$ CoA + acetoacetyl-CoA

Hence, this enzyme has one substrate, acetyl-CoA, and two products, CoA and acetoacetyl-CoA.

Acetyl-CoA C-acetyltransferase belongs to the thiolase family of enzymes.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:acetyl-CoA C-acetyltransferase. Other names in common use include acetoacetyl-CoA thiolase, beta-acetoacetyl coenzyme A thiolase, 2-methylacetoacetyl-CoA thiolase [misleading], 3-oxothiolase, acetyl coenzyme A thiolase, acetyl-CoA acetyltransferase, acetyl-CoA:N-acetyltransferase, and thiolase II. This enzyme participates in 10 metabolic pathways: fatty acid metabolism, synthesis and degradation of ketone bodies, valine, leucine and isoleucine degradation, lysine degradation, tryptophan metabolism, pyruvate metabolism, benzoate degradation via coa ligation, propanoate metabolism, butanoate metabolism, and two-component system - general.

Isozymes

Human genes encoding acetyl-CoA C-acetyltransferases include:

acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A Thiolase) Identifiers Symbol ACAT1 Entrez 38 HUGO 93 OMIM 607809 RefSeq NM_000019 UniProt P24752 Other data EC number 2.3.1.9 Locus Chr. 11 q22.3-23.1

acetyl-Coenzyme A acetyltransferase 2 (acetoacetyl Coenzyme A thiolase) Identifiers Symbol ACAT2 Entrez 39 HUGO 94 OMIM 100678 RefSeq NM_005891 UniProt Q9BWD1 Other data EC number 2.3.1.9 Locus Chr. 6 q25.3-q26

References

1. PDB: 2WKT​; Meriläinen G, Poikela V, Kursula P, Wierenga RK (November 2009). "The thiolase reaction mechanism: the importance of Asn316 and His348 for stabilizing the enolate intermediate of the Claisen condensation". Biochemistry. 48 (46): 11011–25. doi:10.1021/bi901069h. PMID 19842716.

Further reading

• LYNEN F, OCHOA S (1953). "Enzymes of fatty acid metabolism". Biochim. Biophys. Acta. 12 (1-2): 299–314. doi:10.1016/0006-3002(53)90149-8. PMID 13115439.
• Stern JR, Drummond GI, Coon MJ, del Campillo A (1960). "Enzymes of ketone body metabolism. I. Purification of an acetoacetate-synthesizing enzyme from ox liver". J. Biol. Chem. 235: 313–317. PMID 13834445.