Acetyl-CoA C-acetyltransferase

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acetyl-CoA C-acetyltransferase
2WKT.png
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

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

2 acetyl-CoA 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[edit]

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[edit]

  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. PMID 19842716. doi:10.1021/bi901069h. 

Further reading[edit]

  • LYNEN F, OCHOA S (1953). "Enzymes of fatty acid metabolism". Biochim. Biophys. Acta. 12 (1-2): 299–314. PMID 13115439. doi:10.1016/0006-3002(53)90149-8. 
  • 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.