Glycoside hydrolases: catalytic base/nucleophile diversity.
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.
Vuong
Thu V
TV
Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14850, USA.
Wilson
David B
DB
D001419:Bacteria / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008956:Models, Chemical; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
D006026:Glycoside Hydrolases