Synthesis and use of isotope-labelled substrates for a mechanistic study on human alpha-methylacyl-CoA racemase 1A (AMACR; P504S).

@article{Darley2009SynthesisAU,
  title={Synthesis and use of isotope-labelled substrates for a mechanistic study on human alpha-methylacyl-CoA racemase 1A (AMACR; P504S).},
  author={Daniel J. Darley and Danica S Butler and Samuel J Prideaux and Thomas W Thornton and Abigail D Wilson and Timothy J Woodman and Michael D. Threadgill and Matthew D. Lloyd},
  journal={Organic & biomolecular chemistry},
  year={2009},
  volume={7 3},
  pages={543-52}
}
Alpha-Methylacyl-CoA racemase (AMACR) is an important enzyme for the metabolism of branched-chain lipids and drugs. The enzyme is over-expressed in prostate and other cancers. AMACR 1A, the major splice variant, was purified from recombinant E. coli cells as a His-tag protein. Purified enzyme catalysed chiral inversion of both S- and R-2-methyldecanoyl-CoA, with an equilibrium constant of 1.09 +/- 0.14 (2S/2R). Reactions with (2)H-labelled substrate showed that loss of the alpha-proton was a… CONTINUE READING

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