A membrane-bound, calcium-dependent protease in yeast α-cell cleaving on the carboxyl side of paired basic residues

Kensaku Mizuno, Tomoko Nakamura, Katsumi Takada, Shumpei Sakakibara, Hisayuki Matsuo

Research output: Contribution to journalArticlepeer-review

43 Citations (Scopus)

Abstract

Paired basic residues are known as a typical site for proteolytic processing of precursors of bioactive peptides. By using a fluorogenic substrate Boc-Gln-Arg-Arg-MCA, a unique endoprotease exhibiting hydrolytic specificity toward the carboxyl side of paired basic residues was partially purified (about 4600-fold) from the membrane fraction of yeast Saccharomyces cerevisiae α-cells. The enzyme is a calcium-dependent thiol protease, with optimal pH at 7.0. It is a glycoprotein, with an apparent molecular weight of about 100,000-120,000. It cleaves fluorogenic substrates and a synthetic model peptide at the carboxyl side of paired basic residues. From its unique substrate specificity, this enzyme may be involved in precursor processing in vivo.

Original languageEnglish
Pages (from-to)807-814
Number of pages8
JournalBiochemical and biophysical research communications
Volume144
Issue number2
DOIs
Publication statusPublished - 1987 Apr 29
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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