Acetate CoA-transferase

In enzymology, an acetate CoA-transferase (EC 2.8.3.8) is an enzyme that catalyzes the chemical reaction

acetate CoA-transferase
Identifiers
EC no.2.8.3.8
CAS no.37278-35-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
acyl-CoA + acetate a fatty acid anion + acetyl-CoA

Thus, the two substrates of this enzyme are acyl-CoA and acetate, whereas its two products are long-chain carboxylate anion and acetyl-CoA.

This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acyl-CoA:acetate CoA-transferase. Other names in common use include acetate coenzyme A-transferase, butyryl CoA:acetate CoA transferase, butyryl coenzyme A transferase, and succinyl-CoA:acetate CoA transferase.

This enzyme participates in 4 metabolic pathways:

Structural studies

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As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1K6D.

References

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  • Vanderwinkel E, Furmanski P, Reeves HC, Ajl SJ (1968). "Growth of Escherichia coli on fatty acids: requirement for coenzyme A transferase activity". Biochem. Biophys. Res. Commun. 33 (6): 902–8. doi:10.1016/0006-291X(68)90397-5. PMID 4884054.
  • Kaschabek SR, Kuhn B, Muller D, Schmidt E, Reineke W (2002). "Degradation of aromatics and chloroaromatics by Pseudomonas sp strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase". J. Bacteriol. 184 (1): 207–15. doi:10.1128/JB.184.1.207-215.2002. PMC 134768. PMID 11741862.
  • Gobel M, Kassel-Cati K, Schmidt E, Reineke W (2002). "Degradation of aromatics and chloroaromatics by Pseudomonas sp strain B13: cloning, characterization, and analysis of sequences encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase". J. Bacteriol. 184 (1): 216–23. doi:10.1128/JB.184.1.216-223.2002. PMC 134769. PMID 11741863.
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