EC |
2.8.3.8 |
Accepted name: |
acetate CoA-transferase |
Reaction: |
acyl-CoA + acetate = a fatty acid anion + acetyl-CoA |
Other name(s): |
acetate coenzyme A-transferase; butyryl CoA:acetate CoA transferase; butyryl coenzyme A transferase |
Systematic name: |
acyl-CoA:acetate CoA-transferase |
Comments: |
The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism. The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue. Unlike EC 2.8.3.9, butyrate—acetoacetate CoA-transferase, this enzyme exhibits maximal activity using acetate as the CoA acceptor. Substrate range depends on the specific enzyme. Typical substrates include butanoyl-CoA and pentanoyl-CoA. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37278-35-6 |
References: |
1. |
Vanderwinkel, E., Furmanski, P., Reeves, H.C. and Ajl, S.J. Growth of Escherichia coli on fatty acids: requirement for coenzyme A transferase activity. Biochem. Biophys. Res. Commun. 33 (1968) 902–908. [DOI] [PMID: 4884054] |
2. |
Rangarajan, E.S., Li, Y., Ajamian, E., Iannuzzi, P., Kernaghan, S.D., Fraser, M.E., Cygler, M. and Matte, A. Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases. J. Biol. Chem. 280 (2005) 42919–42928. [DOI] [PMID: 16253988] |
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[EC 2.8.3.8 created 1972] |
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