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Alpha-methylacyl-CoA racemase (AMACR) is an enzyme encoded by the AMACR gene that is critical for the metabolism of branched-chain fatty acids and the degradation of certain bile acid intermediates[1][2][5]. AMACR catalyzes the stereoisomeric conversion of (R)- and (S)-methylacyl-CoA, enabling β-oxidation of these substrates in peroxisomes and mitochondria[1][5][6]. It is essential for proper lipid metabolism and has a dual-mitochondrial and peroxisomal localization. Deficiencies in AMACR can lead to metabolic and neurological diseases, while elevated AMACR expression is strongly associated with some cancers, especially prostate cancer, making it a well-established cancer biomarker[5][7]. AMACR also participates in drug metabolism, including metabolism of the NSAID ibuprofen[7]. Its physiological and pathological roles make it a therapeutic target and diagnostic marker in several disease contexts.
Inhibition of AMACR reduces β-oxidation of branched-chain fatty acids and related pathways, potentially lowering growth and survival of certain cancer cells[5][7]. AMACR catalyzes chiral inversion (R-to-S and S-to-R) of α-methylacyl-CoAs, crucial for further metabolic processing[1][2][5][7].
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