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

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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 fromThermoactinomyces vulgaris. Chymostatin and antipain were the most effective inhibitors, with Ki values of 7×10−8 M and 2×10−7 M, 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.

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Authors and Affiliations

  1. Institute of Physiological Chemistry, Martin Luther University Halle-Wittenberg, 4020, Halle/S. Hollystr. 1, GDR

    Dieter Brömme & Rolf Kleine

  2. High School of Engineering, Köthen, GDR

    Rolf Kleine

Authors
  1. Dieter Brömme
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  2. Rolf Kleine
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Brömme, D., Kleine, R. Use of microbial peptide inhibitors for characterization of the substrate specificity of thermitase, a thermostable serine protease fromThermoactinomyces vulgaris . Current Microbiology 11, 317–320 (1984). https://doi.org/10.1007/BF01567698

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