PMID: 4894688Apr 1, 1969Paper

On the mechanism of pepsin action

Proceedings of the National Academy of Sciences of the United States of America
T R Hollands, J S Fruton

Abstract

The problem of the mechanism of pepsin action is considered in relation to recent data on the kinetics and specificity of the enzyme, as well as the finding, reported here, that pepsin exhibits a deuterium isotope effect in the cleavage of a peptide bond. The kinetic parameters for the hydrolysis of the Phe(NO(2))-Phe bond of Gly-Gly-Gly-Phe(NO(2))-Phe-OMe by pepsin have been determined in H(2)O and in D(2)O. The finding of a significant deuterium isotope effect (k(H2O)/k(D2O) = ca. 2) supports the hypothesis that the catalytic mechanism of pepsin involves the participation, in the rate-limiting step, of a proton donor (probably an enzymic carboxyl group) in addition to an enzymic carboxylate group acting as a nucleophile.

References

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Citations

Oct 1, 1970·Archives of Biochemistry and Biophysics·Y Nakagawa, G E Perlmann
Feb 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·I M Voynick, J S Fruton
Apr 15, 1991·Biochemical and Biophysical Research Communications·K L Rebholz, D B Northrop
Sep 1, 1990·Archives of Biochemistry and Biophysics·M S Stack, R D Gray
Jul 11, 2006·Regulatory Toxicology and Pharmacology : RTP·Rod HermanNicholas Storer
Sep 1, 1971·Biochemical and Biophysical Research Communications·L OtvösG Mády
Aug 2, 2003·Biotechnology Progress·Rihab BoushabaNigel K H Slater
Dec 10, 1990·FEBS Letters·A CunninghamT Hofmann

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