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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.

Details

Item Type Articles
CreatorsDarley, D. J., Butler, D. S., Prideaux, S. J., Thornton, T. W., Wilson, A. D., Woodman, T. J., Threadgill, M. D. and Lloyd, M. D.
DOI10.1039/b815396e
DepartmentsFaculty of Science > Pharmacy & Pharmacology
RefereedYes
StatusPublished
ID Code12729

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