Primary structure of the biotin-binding site of chicken liver acetyl-CoA carboxylase

Toshiyuki Takai, Kenji Wada, Tadashi Tanabe

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)98-102
Number of pages5
JournalFEBS Letters
Issue number1
Publication statusPublished - 1987 Feb 9
Externally publishedYes


  • Acetyl-CoA carboxylase
  • Biotin-binding site
  • Nucleotide sequence
  • Primary structure
  • cDNA cloning

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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