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 no.2.3.1.9
CAS no.9027-46-7
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Acetyl-CoA C-acetyltransferase (EC 2.3.1.9) is an enzyme that catalyzes the chemical reaction

2
 
 
 
 
Rightward reaction arrow
 
 
 
 

The enzyme has one substrate, acetyl-CoA, and converts two molecules of this into acetoacetyl-CoA and coenzyme A.[2][3]

Acetyl-CoA C-acetyltransferase has a cysteine at its active site, and is a transferase in the group of acyltransferases which transfer groups other than aminoacyl groups. Its systematic name 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 many metabolic pathways including fatty acid metabolism, synthesis and degradation of ketone bodies, valine, leucine and isoleucine degradation, lysine degradation, tryptophan metabolism, pyruvate metabolism, propanoate metabolism, and butanoate metabolism.[4]

Isozymes

Human genes encoding acetyl-CoA C-acetyltransferases include:

acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A Thiolase)
Identifiers
SymbolACAT1
NCBI gene38
HGNC93
OMIM607809
RefSeqNM_000019
UniProtP24752
Other data
EC number2.3.1.9
LocusChr. 11 q22.3-23.1
Search for
StructuresSwiss-model
DomainsInterPro
acetyl-Coenzyme A acetyltransferase 2 (acetoacetyl Coenzyme A thiolase)
Identifiers
SymbolACAT2
NCBI gene39
HGNC94
OMIM100678
RefSeqNM_005891
UniProtQ9BWD1
Other data
EC number2.3.1.9
LocusChr. 6 q25.3-q26
Search for
StructuresSwiss-model
DomainsInterPro

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.
  2. ↑ 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. S2CID 1546557.
  3. ↑ 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 (2): 313–317. doi:10.1016/S0021-9258(18)69521-3. PMID 13834445.
  4. ↑ Enzyme 2.3.1.9 at KEGG Pathway Database.