title: Unexpected stereoselective exchange of straight-chain fatty acyl-CoA alpha-protons by human alpha-methylacyl-CoA racemase 1A (P504S).
abstract: Alpha-methylacyl-CoA racemase (AMACR; P504S) catalysed exchange of straight-chain fatty acyl-CoA alpha-protons. One alpha-proton was removed in each catalytic cycle, with the pro-S proton preferred. This reaction was most efficient for straight-chain substrates with longer side-chains. 2-Methyldecanoyl-CoA underwent alpha-proton exchange 3x more efficiently (as judged by K(cat)/K(m)) than decanoyl-CoA.
authors.affiliation: Medicinal Chemistry, Department of Pharmacy & Pharmacology, University of Bath, Claverton Down, Bath BA2 7AY, UK.
authors.forename: Fouzia A
authors.initials: FA
authors.lastname: Sattar
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Darley
authors.forename: Francesco
authors.initials: F
authors.lastname: Politano
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Woodman
authors.forename: Michael D
authors.initials: MD
authors.lastname: Threadgill
authors.forename: Matthew D
authors.initials: MD
authors.lastname: Lloyd
mesh_terms: D000214:Acyl Coenzyme A / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D006801:Humans; D015394:Molecular Structure; D011522:Protons; D019998:Racemases and Epimerases / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism
chemical_list: D000214:Acyl Coenzyme A; D011522:Protons; D019998:Racemases and Epimerases; C108352:alpha-methylacyl-CoA racemase