Expression of rat chymotrypsinogen in yeast: A study on the structural and functional significance of the chymotrypsinogen propeptide

István Venekei, László Gráf, William J. Rutter

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The role of the propeptide sequence and a disulfide bridge between sites 1 and 122 in chymotrypsin has been examined by comparing enzyme activities of wild-type and mutant enzymes. The kinetic constants of mutants devoid of the Cys1-Cys122 disulfide-linked propeptide show that this linkage is not important either for activity or substrate specificity. However this linkage appears to be the major factor in keeping the zymogen stable against non-specific activation. A comparison of zymogen stabilities shelved that the trypsinogen propeptide is ten times more effective than tile chymotrypsinogen propeptide in preventing non-specific zymogen activation during heterologous expression and secretion from yeast, This feature can also be transferred in trans to chymotrypsinogen; i.e, the chymotrypsin trypsin propeptide chimera forms a stable zymogen.

Original languageEnglish
Pages (from-to)139-142
Number of pages4
JournalFEBS letters
Volume379
Issue number2
DOIs
Publication statusPublished - Jan 29 1996

Keywords

  • Chymotrypsin
  • Disulfide bond
  • Protein folding
  • Zymogen activation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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