Two enzymes concerned in peptide hormone α-amidation are synthesized from a single mRNA

Ichiro Kato, Hideto Yonekura, Masahiro Tajima, Mitsuo Yanagi, Hiroshi Yamamoto, Hiroshi Okamoto

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

By expressing truncated rat pituitary 'peptidylglycine α-amidating enzyme' cDNAs in COS-7 cells, we found that the two reactions concerned in peptide carboxyl-terminal amidation, namely the peptidylglycine α-hydroxylation reaction and the peptidyl-hydroxyglycine amidation reaction, were catalyzed by 37-and 53-K proteins, which were derived from the 5′- and 3′-coding sequences, respectively. The full-length cDNA directed the expression of both the 37- and 53-K enzymes, and in the combined presence of the two enzymes the full conversion of a glycine-extended peptide into the amidated product was achieved. These results indicated that two enzymes concerned in peptide hormone α-amidation are generated from a common precursor protein encoded by a single mRNA.

Original languageEnglish
Pages (from-to)197-203
Number of pages7
JournalBiochemical and biophysical research communications
Volume172
Issue number1
DOIs
Publication statusPublished - 1990 Oct 15

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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