Quantitative estimation of activities of mutant enzymes

Research output: Contribution to journalArticle

9 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)185-190
Number of pages6
JournalCatalysis Letters
Volume2
Issue number3
DOIs
Publication statusPublished - May 1989

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Serine Proteases
Amino acids
enzymes
Enzymes
Amino Acids
protease
Water
Substrates
amino acids
polarity
predictions
water
Peptide Hydrolases

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Catalysis

Cite this

Quantitative estimation of activities of mutant enzymes. / Náray-Szabó, G.

In: Catalysis Letters, Vol. 2, No. 3, 05.1989, p. 185-190.

Research output: Contribution to journalArticle

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