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Article

Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis. Mutational and structural characterization of the active site and the fold.

The Journal of biological chemistry - 1 Apr 2005

Savolainen Kalle, Bhaumik Prasenjit, Schmitz Werner, Kotti Tiina J, Conzelmann Ernst, Wierenga Rik K, Hiltunen J Kalervo

Abstract excerpt

Alpha-methylacyl-CoA racemase (Amacr) catalyzes the racemization of alpha-methyl-branched CoA esters. Sequence comparisons have shown that this enzyme is a member of the family III CoA transferases. The mammalian Amacr is involved in bile acid synthesis and branched-chain fatty acid degradation. In human, mutated variants of Amacr have been shown to be associated with disease states. Amino acid sequence alignment...

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PMID: 15632186
DOI: 10.1074/jbc.M409704200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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