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

Reference:

Darley, D. J., Butler, D. S., Prideaux, S. J., Thornton, T. W., Wilson, A. D., Woodman, T. J., Threadgill, M. D. and Lloyd, M. D., 2009. Synthesis and use of isotope-labelled substrates for a mechanistic study on human α-methylacyl-CoA racemase 1A (AMACR; P504S). Organic and Biomolecular Chemistry, 7 (3), pp. 543-552.

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Official URL:

http://dx.doi.org/10.1039/b815396e

Abstract

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 H-2-labelled substrate showed that loss of the alpha-proton was a prerequisite for chiral inversion. Reactions conducted in (H2O)-H-2 indicated that reprotonation was not stereospecific. These results are the first mechanistic study on any recombinant mammalian alpha-methylacyl-CoA racemase.

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