Molecular basis of acyl-CoA ester recognition by α-methylacyl-CoA racemase from Mycobacterium tuberculosis.

ABSTRACT: α-Methylacyl-CoA racemase (AMACR; P504S) enzyme plays a vital role in branched-chain fatty acid metabolism by catalyzing the conversion of 2-methyl-branched fatty acyl-CoAs into a near 1 to 1 mixture of the (2R)- and (2S)-epimers, enabling further metabolism. α-Methylacyl-CoA racemase from Mycobacterium tuberculosis (MCR) has been explored as a model to understand the AMACR racemization mechanism and as a drug target. Here we present a detailed analysis of a new MCR wild-type crystal structure to provide insights into the MCR racemization mechanism and the molecular features that contribute enzyme activity and selectivity. Specifically, we report a structure of wild-type MCR (in tetragonal space group I422, a new crystal form) along with 12 structures of MCR in complex with branched-chain

SUBMITTER: Mojanaga OO 

PROVIDER: S-EPMC12246613 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature