Cloning and sequence of cDNA encoding a peptide C-terminal α-amidating enzyme from Xenopus laevis

Kensaku Mizuno, Kazuhiro Ohsuye, Yayoi Wada, Kayoko Fuchimura, Shoji Tanaka, Hisayuki Matsuo

Research output: Contribution to journalArticlepeer-review

61 Citations (Scopus)

Abstract

The C-terminal α-amide formation of the peptides is one of the most important events of prohormone processing. We have recently isolated an α-amidating enzyme, AE-I, from Xenopus laevis skin, which is the only enzyme ever purified to homogeneity. In this study, we report cloning and sequence of cDNA encoding AE-I. Our results indicate that enzyme AE-I is initially synthesized as a precursor with 400 amino acid residues, which is further processed to the mature enzyme consisting of 344 residues. Preliminary expression in E. coli of the cDNA corresponding to AE-I was found to produce an enzyme with appreciable α-amidating activity.

Original languageEnglish
Pages (from-to)546-552
Number of pages7
JournalBiochemical and biophysical research communications
Volume148
Issue number2
DOIs
Publication statusPublished - 1987 Oct 29
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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