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Publication : Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substrates.

First Author  Hsiao YS Year  2006
Journal  J Biol Chem Volume  281
Issue  38 Pages  28480-7
PubMed ID  16870616 Mgi Jnum  J:116933
Mgi Id  MGI:3695239 Doi  10.1074/jbc.M602622200
Citation  Hsiao YS, et al. (2006) Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substrates. J Biol Chem 281(38):28480-7
abstractText  Carnitine acyltransferases catalyze the reversible exchange of acyl groups between coenzyme A (CoA) and carnitine. They have important roles in many cellular processes, especially the oxidation of long-chain fatty acids in the mitochondria for energy production, and are attractive targets for drug discovery against diabetes and obesity. To help define in molecular detail the catalytic mechanism of these enzymes, we report here the high resolution crystal structure of wild-type murine carnitine acetyltransferase (CrAT) in a ternary complex with its substrates acetyl-CoA and carnitine, and the structure of the S554A/M564G double mutant in a ternary complex with the substrates CoA and hexanoylcarnitine. Detailed analyses suggest that these structures may be good mimics for the Michaelis complexes for the forward and reverse reactions of the enzyme, representing the first time that such complexes of CrAT have been studied in molecular detail. The structural information provides significant new insights into the catalytic mechanism of CrAT and possibly carnitine acyltransferases in general.
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