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FEBS Lett. 2000 Jan 28;466(2-3):239-43.

cDNA-derived amino acid sequence of acetoacetyl-CoA synthetase from rat liver.

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Department of Health Chemistry, Faculty of Pharmaceutical Sciences, Hoshi University, Tokyo, Japan.


In order to examine the primary structure of acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, EC; AA-CoA synthetase), the cDNA clone encoding this enzyme has been isolated from the cDNA library which was prepared from the liver of rat fed a diet supplemented with 4% cholestyramine and 0.4% pravastatin for 4 days. Nucleotide sequence analysis of cloned cDNA revealed that AA-CoA synthetase of rat liver contains an open reading frame of 2019 nucleotides, and the deduced amino acid sequence (672 amino acid residues) bears 25.0 and 38.9% homologies with acetyl-CoA synthetases of Saccharomyces cerevisiae and Archaeoglobus fulgidus, respectively.

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