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Glycoside hydrolases: Catalytic base/nucleophile diversity
Author(s) -
Vuong Thu V.,
Wilson David B.
Publication year - 2010
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.22838
Subject(s) - nucleophile , catalysis , glycoside hydrolase , chemistry , substrate (aquarium) , hydrolase , stereochemistry , carboxylate , enzyme , glycoside , function (biology) , combinatorial chemistry , biochemistry , biology , ecology , genetics
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.