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Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin

Nature volume 221, pages 337–340 (1969)Cite this article

Abstract

The catalytic site of chymotrypsin contains an interior aspartic acid hydrogen-bonded to a histidine which in its turn is hydrogen-bonded to a serine. Polarization of the system due to the buried negative charge of the aspartic acid residue would make the serine oxygen strongly nucleophilic and would explain its reactivity towards amides and esters.

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Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Cambridge

    D. M. BLOW, J. J. BIRKTOFT & B. S. HARTLEY

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  1. D. M. BLOW
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  2. J. J. BIRKTOFT
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  3. B. S. HARTLEY
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BLOW, D., BIRKTOFT, J. & HARTLEY, B. Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin. Nature 221, 337–340 (1969). https://doi.org/10.1038/221337a0

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