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Stereochemistry of Substrate Binding and Hydrolysis in the Trypsin Family of Enzymes

  • Conference paper
Proteinase Inhibitors

Part of the book series: Bayer-Symposium ((BAYER-SYMP,volume 5))

Abstract

This introductory review aims to describe the three-dimensional molecular structure found at the active site of crystalline trypsin and its homologues; to show how small substrate analogues and inhibitors have been found to interact with the active site of crystals; to relate these structural observations to our knowledge of the specificity of these enzymes; and to indicate how they can be reconciled with our ideas of the catalytic mechanism.

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Author information

Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Cambridge, CB2 2QH, Great Britain

    D. M. Blow

Authors
  1. D. M. Blow
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Editor information

Editors and Affiliations

  1. Institut für Klinische Chemie und Klinische Biochemie, Universität München, 8000, Munich 2, Fed. Rep. Germany

    Hanz Fritz

  2. Organisch-Chemisches Laboratorium, Technischen Universität München, 8000, Munich 2, Fed. Rep. Germany

    Harald Tschesche

  3. Department of Biology, Brookhaven National Laboratory, Upton, NY, 11973, USA

    Lewis J. Greene

  4. Biochemisches Laboratorium, Bayer AG, 5600, Wuppertal 1, Fed. Rep. Germany

    Ernst Truscheit (Editor-in-Chief) (Editor-in-Chief)

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© 1974 Springer-Verlag

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Blow, D.M. (1974). Stereochemistry of Substrate Binding and Hydrolysis in the Trypsin Family of Enzymes. In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds) Proteinase Inhibitors. Bayer-Symposium, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87966-1_53

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  • DOI: https://doi.org/10.1007/978-3-642-87966-1_53

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-87968-5

  • Online ISBN: 978-3-642-87966-1

  • eBook Packages: Springer Book Archive

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