Peptidylglycine α-amidating reaction: Evidence for a two-step mechanism involving a stable intermediate at neutral pH

Kenichi Takahashi, Hiroshi Okamoto, Hiroshi Seino, Masato Noguchi

研究成果: Article査読

65 被引用数 (Scopus)

抄録

In our previous study of the rat brain α-amidating activity, we suggested that a protein of 41 kdal (41K protein) that shows no α-amidating activity is required for the reaction at neutral pH in addition to an α-amidating enzyme of 36 kdal(36K enzyme). Here we report on the purification of both proteins to near homogeneity and provide evidence that α-amidation proceeds via a two-step mechanism involving a stable intermediate at neutral pH, which is initially formed by the 36K enzyme and then readily converted into an amide product by the 41K protein.

本文言語English
ページ(範囲)524-530
ページ数7
ジャーナルBiochemical and biophysical research communications
169
2
DOI
出版ステータスPublished - 1990 6 15

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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