Experimental support for Asp-52's importance in lysozyme using a carbohydrate-based enzyme model. Acetal hydrolysis catalyzed by a "stereoelectronically correct" carboxylate group

Theories concerning the mechanism of action of lysozyme and the testing of those theories by enzyme modelling efforts are amongst the most thoroughly documented in the bioorganic literature. It is at least fair to say that the role of Asp-52 in lysozyme remains one of the most long-lived enigmas in...

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Bibliographic Details
Published in:Journal of the American Chemical Society 1988-09, Vol.110 (19), p.6566-6568
Main Authors: Cherian, Xavier M, Van Arman, Scott A, Czarnik, Anthony W
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
enzyme models
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
lysozyme
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Summary:Theories concerning the mechanism of action of lysozyme and the testing of those theories by enzyme modelling efforts are amongst the most thoroughly documented in the bioorganic literature. It is at least fair to say that the role of Asp-52 in lysozyme remains one of the most long-lived enigmas in enzyme mechanism chemistry. The authors now report that the hydrolysis of riboside ketal, slowed by steric inhibition to "backside" solvation, is accelerated by a factor of 860 upon introduction of a carboxylate group.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja00227a049