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

Authors :
Iwahori A
Takahashi N
Nakamoto M
Iwama M
Fukui T
Source :
FEBS letters [FEBS Lett] 2000 Jan 28; Vol. 466 (2-3), pp. 239-43.
Publication Year :
2000

Abstract

In order to examine the primary structure of acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, EC 6.2.1.16; 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.

Details

Language :
English
ISSN :
0014-5793
Volume :
466
Issue :
2-3
Database :
MEDLINE
Journal :
FEBS letters
Publication Type :
Academic Journal
Accession number :
10682835
Full Text :
https://doi.org/10.1016/s0014-5793(99)01794-9