Unexpected stereoselective exchange of straight-chain fatty acyl-CoA alpha-protons by human alpha-methylacyl-CoA racemase 1A (P504S).
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.
Sattar
Fouzia A
FA
Medicinal Chemistry, Department of Pharmacy & Pharmacology, University of Bath, Claverton Down, Bath BA2 7AY, UK.
Darley
Daniel J
DJ
Politano
Francesco
F
Woodman
Timothy J
TJ
Threadgill
Michael D
MD
Lloyd
Matthew D
MD
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
D000214:Acyl Coenzyme A; D011522:Protons; D019998:Racemases and Epimerases; C108352:alpha-methylacyl-CoA racemase