IUBMB Enzyme Nomenclature


Accepted name: acyl-CoA:acyl-CoA alkyltransferase

Reaction: 2 an acyl-CoA + H2O = a (2R)-2-alkyl-3-oxoalkanoate + 2 CoA

Other name(s): oleA (gene name)

Systematic name: acyl-CoA:acyl-CoA alkyltransferase [(2R)-2-alkyl-3-oxoalkanoate-forming]

Comments: The enzyme, found in certain bacterial species, catalyses a head-to-head non-decarboxylative Claisen condensation of two acyl-CoA molecules, resulting in formation of a 2-alkyl-3-oxoalkanoic acid. It is part of a pathway for the production of olefins.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:


1. Sukovich, D.J., Seffernick, J.L., Richman, J.E., Hunt, K.A., Gralnick, J.A. and Wackett, L.P. Structure, function, and insights into the biosynthesis of a head-to-head hydrocarbon in Shewanella oneidensis strain MR-1. Appl. Environ. Microbiol. 76 (2010) 3842-3849. [PMID: 20418444]

2. Frias, J.A., Richman, J.E., Erickson, J.S. and Wackett, L.P. Purification and characterization of OleA from Xanthomonas campestris and demonstration of a non-decarboxylative Claisen condensation reaction. J. Biol. Chem. 286 (2011) 10930-10938. [PMID: 21266575]

3. Goblirsch, B.R., Frias, J.A., Wackett, L.P. and Wilmot, C.M. Crystal structures of Xanthomonas campestris OleA reveal features that promote head-to-head condensation of two long-chain fatty acids. Biochemistry 51 (2012) 4138-4146. [PMID: 22524624]

4. Goblirsch, B.R., Jensen, M.R., Mohamed, F.A., Wackett, L.P. and Wilmot, C.M. Substrate trapping in crystals of the thiolase OleA identifies three channels that enable long chain olefin biosynthesis. J. Biol. Chem. 291 (2016) 26698-26706. [PMID: 27815501]

[EC created 2018]

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