Catalysis Letters

, Volume 2, Issue 3, pp 185–190 | Cite as

Quantitative estimation of activities of mutant enzymes

  • Gábor Náray-Szabó
Article

Abstract

A simple equation is presented for the prediction of catalytic efficiencies and Michaelis constants for pairs of mutant serine proteases and substrates with variable P1 side chains. The equation is a generalization of the “similis simili gaudet” principle formulated by Gráf et al. [3] (Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 4961, stating that in water amino-acid side chains with similar polarities tend to Interact stronger than dissimilar ones.

Keywords

Enzyme Physical Chemistry Catalysis Serine Serine Protease 

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Copyright information

© J.C. Baltzer A.G. Scientific Publishing Company 1989

Authors and Affiliations

  • Gábor Náray-Szabó
    • 1
  1. 1.CHINOIN Pharmaceutical and Chemical WorksBudapestHungary

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