Glycoside hydrolases: Catalytic base/nucleophile diversity |
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Authors: | Thu V. Vuong David B. Wilson |
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Affiliation: | 1. Department of Molecular Biology and Genetics, Cornell University, 458 Biotechnology Building, Ithaca, New York 14850;2. telephone: 607‐255‐5706;3. fax: 607‐255‐2428 |
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Abstract: | ![]() Recent studies have shown that a number of glycoside hydrolase families do not follow the classical catalytic mechanisms, as they lack a typical catalytic base/nucleophile. A variety of mechanisms are used to replace this function, including substrate‐assisted catalysis, a network of several residues, and the use of non‐carboxylate residues or exogenous nucleophiles. Removal of the catalytic base/nucleophile by mutation can have a profound impact on substrate specificity, producing enzymes with completely new functions. Biotechnol. Bioeng. 2010;107: 195–205. © 2010 Wiley Periodicals, Inc. |
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Keywords: | glycoside hydrolases catalytic mechanism catalytic base nucleophile diversity |
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