Interaction between Chymotrypsin (Trypsin) and the Pancreatic Trypsin Inhibitor (Kallikrein Inactivator)

  • R. Huber
Conference paper
Part of the Colloquium der Gesellschaft für Biologische Chemie 13.–15. April 1972 in Mosbach/Baden book series (MOSBACH, volume 23)

Abstract

The high velocity of enzymatic reactions is ascribed to the proximity of the catalytic groups and the substrate within the rigid enzyme substrate complex. Translational and rotational degrees of freedom are frozen out within the complex and the reactive centres favourably oriented [1–4]. Furtheron the geometric arrangement of the reactants involved in the catalytic reaction might be stabilized in a steric conformation closely resembling that of the transition state of the reaction [5, 6]. These factors may increase the velocity of enzymatic reactions by many orders of magnitude over their non-enzymatic analogs.

Keywords

Hydrolysis Glycine Serine Proline Lysine 

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Copyright information

© Springer-Verlag Berlin · Heidelberg 1972

Authors and Affiliations

  • R. Huber
    • 1
  1. 1.Max-Planck-Institut für Eiweiß- und Lederforschung und Physikalisch-Chemisches Institut der TechnischenUniversität MünchenGermany

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