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Mechanism of acid protease catalysis based on the crystal structure of penicillopepsin.

作者信息

James M N, Hsu I N, Delbaere L T

出版信息

Nature. 1977 Jun 30;267(5614):808-13. doi: 10.1038/267808a0.

DOI:10.1038/267808a0
PMID:895839
Abstract

A proposed mechanism for the catalytic hydrolysis of peptide bonds by acid proteases is similar in many respects to the Zn-carbonyl mechanism previously derived for carboxypeptidase A. In the acid proteases the electrophilic component is the proton shared by Asp-32 and Asp-215; Tyr-75 donates its proton to the amide nitrogen of the scissile bond and an OH- ion from a water molecule bound between the carboxyl group of Asp-32 and the substrate attacks the carbonyl carbon atom.

摘要

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