Electrostatic catalysis in enzymes

Research output: Contribution to journalArticle

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Abstract

Arguments are presented for the importance of electrostatics in enzyme catalysis. Theoretical calculations and specially designed experiments on serine proteases indicate that the protein electrostatic field stabilises the strongly polar transition intermediate and thus enhances the reaction rate. Similar theoretical conclusions have also been drawn for other enzymes. A hypothesis is outlined stating that specificity is enhanced if the interacting groups of the enzyme and its substrate in the transition state are of similar nature, i.e. if both are ionic, polar or apolar. The statement is supported by published experimental data from site-directed mutagenesis studies.

Original languageEnglish
Pages (from-to)281-287
Number of pages7
JournalJournal of Molecular Catalysis
Volume47
Issue number2-3
DOIs
Publication statusPublished - Sep 26 1988

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Catalysis
Electrostatics
Enzymes
Mutagenesis
Reaction rates
Electric fields
Proteins
Substrates
Experiments
Peptide Hydrolases

ASJC Scopus subject areas

  • Engineering(all)

Cite this

Electrostatic catalysis in enzymes. / Náray-Szabó, G.

In: Journal of Molecular Catalysis, Vol. 47, No. 2-3, 26.09.1988, p. 281-287.

Research output: Contribution to journalArticle

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