Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces, cerevisiae

Kensaku Mizuno, Tomoko Nakamura, Takehiro Ohshima, Shoji Tanaka, Hisayuki Matsuo

Research output: Contribution to journalArticle

69 Citations (Scopus)

Abstract

Yeast Saccharomyces, cerevisiae, KEX2 gene previously isolated was characterized as the gene encoding an endopeptidase required for proteolytic processing of precursors of α-factor and killer toxin. In this study, the cloned KEX2 gene was introduced into the kex2 mutant cells and the KEX2 gene product expressed in these cells was partially purified from their membrane fraction. The enzyme preparation exhibits a calcium-dependent endopeptidase activity with a substrate specificity toward the carboxyl side of Lys-Arg, Arg-Arg and Pro-Arg sequences. The enzyme activity was inhibited by serine-protease inhibitors, such as DFP and PMSF, indicating that the KEX2 endopeptidase belongs to a serine-protease family. The optimal pH was determined to be around 5.5. Thus, the KEX2 endopeptidase was found to be a unique calcium-dependent serine-protease distinct from calpain and trypsin.

Original languageEnglish
Pages (from-to)305-311
Number of pages7
JournalBiochemical and biophysical research communications
Volume159
Issue number1
DOIs
Publication statusPublished - 1989 Feb 28
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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