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Inhibition of Human α‐Methylacyl CoA Racemase (AMACR): a Target for Prostate Cancer
Author(s) -
Carnell Andrew J.,
Kirk Ralph,
Smith Matthew,
McKenna Shane,
Lian LuYun,
Gibson Robert
Publication year - 2013
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201300179
Subject(s) - prostate cancer , enzyme , cancer , kidney cancer , hek 293 cells , chemistry , cancer research , prostate , biochemistry , biology , medicine , gene
Abstract The enzyme α‐methylacyl CoA racemase (AMACR) is involved in the metabolism of branched‐chain fatty acids and has been identified as a promising therapeutic target for prostate cancer. By using the recently available human AMACR from HEK293 kidney cell cultures, we tested a series of new rationally designed inhibitors to determine the structural requirements in the acyl component. An N ‐methylthiocarbamate ( K i =98 n M ), designed to mimic the proposed enzyme‐bound enolate, was found to be the most potent AMACR inhibitor reported to date.