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Primary structure of the biotin‐binding site of chicken liver acetyl‐CoA carboxylase
Author(s) -
Takai Toshiyuki,
Wada Kenji,
Tanabe Tadashi
Publication year - 1987
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 - 10.1016/0014-5793(87)81564-8
Subject(s) - pyruvate carboxylase , biotin , acetyl coa carboxylase , biochemistry , biology , peptide sequence , protein primary structure , microbiology and biotechnology , nucleic acid sequence , proteolysis , serine , enzyme , dna , gene
Limited proteolysis of chicken liver acetyl‐CoA carboxylase by staphylococcal serine proteinase yielded a fragment of 31 kDa which contained the biotinyl active site. This polypeptide was purified by preparative polyacrylamide gel electrophoresis and characterized. The complete amino acid sequence of this polypeptide has been deduced from the nucleotide sequence of cloned DNA complementary to the chicken liver acetylCoA carboxylase mRNA. A highly conserved sequence of Met‐Lys‐Met was found in the biotin‐binding site. Appreciable homology was observed among the sequences in close vicinity of the biotin sites of chicken liver acetyl‐CoA carboxylase and other biotin‐dependent carboxylases including biotin carboxyl carrier protein of Escherichia coli acetyl‐CoA carboxylase.