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cDNA‐derived amino acid sequence of acetoacetyl‐CoA synthetase from rat liver 1
Author(s) -
Iwahori Akiyo,
Takahashi Noriko,
Nakamoto Mayumi,
Iwama Masanori,
Fukui Tetsuya
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01794-9
Subject(s) - complementary dna , biochemistry , microbiology and biotechnology , peptide sequence , nucleic acid sequence , amino acid , biology , protein primary structure , open reading frame , dna ligase , cdna library , enzyme , gene
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.