[HTML][HTML] α-Methylacyl-CoA Racemase from Mycobacterium tuberculosis: MUTATIONAL AND STRUCTURAL CHARACTERIZATION OF THE ACTIVE SITE AND THE …
K Savolainen, P Bhaumik, W Schmitz, TJ Kotti… - Journal of Biological …, 2005 - ASBMB
α-Methylacyl-CoA racemase (Amacr) catalyzes the racemization of α-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 of Amacrs and its
homologues from various species revealed 26 conserved protic residues, assumed to be …
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 of Amacrs and its
homologues from various species revealed 26 conserved protic residues, assumed to be …