Characterization of an Aspergillus oryzae cysteinyl dipeptidase expressed in Escherichia coli

Biosci Biotechnol Biochem. 2011;75(1):159-61. doi: 10.1271/bbb.100604. Epub 2011 Jan 7.

Abstract

Cysteinyl dipeptidase from Aspergillus oryzae (CdpA) was produced in Escherichia coli and purified. The enzyme showed activity specific toward cysteine-containing dipeptides, but its substrate specificity was distinct from those of other cysteinyl dipeptidases of the M20 family. It was optimally active at pH 7-8 and stable at pH 6-9 and at up to 40 °C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus oryzae / enzymology*
  • Cloning, Molecular
  • Cysteine / metabolism*
  • Dipeptidases / biosynthesis
  • Dipeptidases / genetics*
  • Dipeptidases / isolation & purification
  • Dipeptidases / metabolism*
  • Escherichia coli / genetics*
  • Gene Expression
  • Humans
  • Oligopeptides / metabolism
  • Substrate Specificity

Substances

  • Oligopeptides
  • Dipeptidases
  • dipeptidase
  • Cysteine