Rates of Uncatalyzed Peptide Bond Hydrolysis in Neutral Solution and the Transition State Affinities of Proteases

Anna Radzicka; Richard Wolfenden

doi:10.1021/ja954077c

journal article Jan 01, 1996

Rates of Uncatalyzed Peptide Bond Hydrolysis in Neutral Solution and the Transition State Affinities of Proteases

Anna Radzicka Richard Wolfenden

Journal of the American Chemical Society Vol. 118 No. 26 pp. 6105-6109 · American Chemical Society (ACS)

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The present rate constant for hydrolysis of the peptide bond in AcGG, obtained by extrapolation to 25 °C and pH 7, is 2 × 10-11s-1, considerably lower than the rate constant (3 × 10-9s-1) reported earlier by Kahne and Still5for release of C-terminal glycine from a tetrapeptide (-Phe-Phe-Phe-Gly) joined through its N-terminus to a polyacrylamide resin. The nature of the peptide bond undergoing cleavage is similar in these two reactions; and steric hindrance, if any, seems more likely to have occurred in the case of the resin-bound peptide. This suggests the possibility that attack by water on the resin-bound peptide might be assisted by its proximity to the polymer matrix, directly or through some effect on the solvent environment.

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Details

Published: Jan 01, 1996
Vol/Issue: 118(26)
Pages: 6105-6109

Authors

A

Anna Radzicka

Contribution from the Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599

R

Richard Wolfenden

Contribution from the Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599

Cite This Article

Anna Radzicka, Richard Wolfenden (1996). Rates of Uncatalyzed Peptide Bond Hydrolysis in Neutral Solution and the Transition State Affinities of Proteases. Journal of the American Chemical Society, 118(26), 6105-6109. https://doi.org/10.1021/ja954077c

Rates of Uncatalyzed Peptide Bond Hydrolysis in Neutral Solution and the Transition State Affinities of Proteases

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