title: Glycoside hydrolases: catalytic base/nucleophile diversity.
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.
authors.affiliation: Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14850, USA.
authors.forename: Thu V
authors.initials: TV
authors.lastname: Vuong
authors.forename: David B
authors.initials: DB
authors.lastname: Wilson
mesh_terms: 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
chemical_list: D006026:Glycoside Hydrolases