Inhibition of Human α‐Methylacyl CoA Racemase (AMACR): a Target for Prostate Cancer. Issue 10 (8th August 2013)

• Record Type: Journal Article
• Authors: Carnell, Andrew J.; Kirk, Ralph; Smith, Matthew; McKenna, Shane; Lian, Lu‐Yun; Gibson, Robert
• Is Part Of: ChemMedChem. Volume 8:Issue 10(2013:Oct.)
• Page Start: 1643
• Page End: 1647
• Publication Date: 2013-08-08
• Subjects: Pharmaceutical chemistry -- Periodicals; 615.19005
• DOI: 10.1002/cmdc.201300179
• Languages: English
• ISSNs: 1860-7179

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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 <italic>N</italic>‐methylthiocarbamate (<italic>K</italic>_i=98 n<sc>M</sc>), designed to mimic the proposed enzyme‐bound enolate, was found to be the most potent AMACR inhibitor reported to date.</p> </abstract>