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Propeptide-Mediated Folding in Subtilisin: The Intramolecular Chaperone Concept

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Subtilisin Enzymes

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 379))

Abstract

Subtilisin, an alkaline serine protease consisting of 275 amino acid residues is produced in various strains of Bacillus 1. As it was first identified in B. subtilis the enzyme was named ‘subtilisin’. Different variants of this enzyme have been identified and well studied. Among these include subtilisin BPN’, subtilisin E and subtilisin Carlsberg. Later this exoenzyme was found to belong to a very large family of proteins spanning both prokaryotes and eukaryotes called subtilases2.

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Author information

Authors and Affiliations

  1. Department of Biochemistry, University of Medicine and Dentistry of New Jersey Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ, 08854, USA

    Ujwal Shinde & Masayori Inouye

Authors
  1. Ujwal Shinde
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  2. Masayori Inouye
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Editor information

Editors and Affiliations

  1. Genecor International, Inc., South San Francisco, California, USA

    Richard Bott

  2. European Molecular Biology Laboratory, Hamburg, Germany

    Christian Betzel

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© 1996 Plenum Press, New York

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Shinde, U., Inouye, M. (1996). Propeptide-Mediated Folding in Subtilisin: The Intramolecular Chaperone Concept. In: Bott, R., Betzel, C. (eds) Subtilisin Enzymes. Advances in Experimental Medicine and Biology, vol 379. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0319-0_16

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  • DOI: https://doi.org/10.1007/978-1-4613-0319-0_16

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-306-45108-9

  • Online ISBN: 978-1-4613-0319-0

  • eBook Packages: Springer Book Archive

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