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

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)524-530
Number of pages7
JournalBiochemical and biophysical research communications
Volume169
Issue number2
DOIs
Publication statusPublished - 1990 Jun 15

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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