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

Toshiyuki Takai, Kenji Wada, Tadashi Tanabe

研究成果: Article査読

10 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)98-102
ページ数5
ジャーナルFEBS Letters
212
1
DOI
出版ステータスPublished - 1987 2月 9
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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