Zymogen activation confers thermodynamic stability on a key peptide bond and protects human cationic trypsin from degradation

András Szabó, Evette S. Radisky, Miklós Sahin-Tóth

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

Background: Initial cleavage by chymotrypsin C regulates degradation of human cationic trypsin. Results: Cleavage is reversible and favors calcium-dependent bond formation in trypsin, but not in trypsinogen. Conclusion: Trypsin resistance to degradation derives from the regulated thermodynamic stability of a specific peptide bond that is responsive to physiological environment. Significance: This new paradigm explains the robustness of trypsin functioning in the protease-rich intestinal milieu.

Original languageEnglish (US)
Pages (from-to)4753-4761
Number of pages9
JournalJournal of Biological Chemistry
Volume289
Issue number8
DOIs
StatePublished - Feb 21 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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