Haloenol lactones: enzyme-activated irreversible inactivators for serine proteases. Inactivation of alpha-chymotrypsin.

P. K. Chakravarty, G. A. Krafft, J. A. Katzenellenbogen

Research output: Contribution to journalArticlepeer-review

Abstract

Two haloenol lactones have been shown to inactivate alpha-chymotrypsin by an enzyme-mediated process. According to the postulated mechanism, acylation of the active site serine by the haloenol lactone reveals an alpha-haloketone, which alkylates the enzyme at the active site and renders the enzyme inactive. The inactivation has been shown to require enzymatic activation of the inhibitor to its reactive form to take place within the acyl-enzyme intermediate and to be irreversible.

Original languageEnglish (US)
Pages (from-to)610-612
Number of pages3
JournalJournal of Biological Chemistry
Volume257
Issue number2
StatePublished - Jan 25 1982

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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