Use of microbial peptide inhibitors for characterization of the substrate specificity of thermitase, a thermostable serine protease from Thermoactinomyces vulgaris

Dieter Brömme, Rolf Kleine

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Seven microbial peptide inhibitors-chymostatin, antipain, elastatinal, leupeptin, pepstatin, bestatin, and phosphoramidon-were tested for their efficiency to inhibit thermitase, a thermostable serine protease from Thermoactinomyces vulgaris. Chymostatin and antipain were the most effective inhibitors, with Ki values of 7×10-8M and 2×10-7M, respectively. Except for leupeptin, all inhibitors resist hydrolysis by thermitase. Leupeptin, however, is cleaved by thermitase between the two leucylresidues. Further, a close relationship in specificity between thermitase and subtilisin BPN′ and their distinct discrimination from elastase specificity was demonstrated by using these inhibitors.

Original languageEnglish
Pages (from-to)317-320
Number of pages4
JournalCurrent Microbiology
Volume11
Issue number6
DOIs
StatePublished - Nov 1984
Externally publishedYes

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