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

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Contribution from the Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599
Cite this: J. Am. Chem. Soc. 1996, 118, 26, 6105–6109
Publication Date (Web):July 3, 1996
https://doi.org/10.1021/ja954077c
Copyright © 1996 American Chemical Society
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    Abstract

    To assess the relative proficiencies of enzymes that catalyze the hydrolysis of internal and C-terminal peptide bonds, the rates of the corresponding nonenzymatic reactions were examined at elevated temperatures in sealed quartz tubes, yielding linear Arrhenius plots. The results indicate that in neutral solution at 25 °C, peptide bonds are hydrolyzed with half-times of approximately 500 years for the C-terminal bond of acetylglycylglycine, 600 years for the internal peptide bond of acetylglycylglycine N-methylamide, and 350 years for the dipeptide glycylglycine. These reactions, insensitive to changing pH or ionic strength, appear to represent uncatalyzed attack by water on the peptide bond. Comparison of rate constants indicates very strong binding of the altered substrate in the transition states for the corresponding enzyme reactions, Ktx attaining a value of less than 10-17 M in carboxypeptidase B. The half-life of the N-terminal peptide bond in glycylglycine N-methylamide, whose hydrolysis might have provided a reference for assessing the catalytic proficiency of an aminopeptidase, could not be determined because this compound undergoes relatively rapid intramolecular displacement to form diketopiperazine (t1/2 ∼ 35 days at pH 7 and 37 °C). The speed of this latter process suggests an evolutionary rationale for posttranslational N-acetylation of proteins in higher organisms, as a protection against rapid degradation.

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    †

     Present address:  3-Dimensional Pharmaceuticals, Inc., 665 Stockton Drive, Exton, PA 19341.

    *

    In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

    ✗

     Abstract published in Advance ACS Abstracts, June 15, 1996.

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