The Enzyme Database

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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
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 27815501]
[EC created 2018]

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