Unexpected stereoselective exchange of straight-chain fatty acyl-CoA alpha-protons by human alpha-methylacyl-CoA racemase 1A (P504S)

Chem Commun (Camb). 2010 May 21;46(19):3348-50. doi: 10.1039/c002509g. Epub 2010 Mar 30.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / chemistry
  • Acyl Coenzyme A / metabolism*
  • Biocatalysis
  • Humans
  • Molecular Structure
  • Protons*
  • Racemases and Epimerases / chemistry
  • Racemases and Epimerases / metabolism*
  • Stereoisomerism

Substances

  • Acyl Coenzyme A
  • Protons
  • Racemases and Epimerases
  • alpha-methylacyl-CoA racemase