title: Sweetly expanding enzymatic glycodiversification.
abstract: Directed evolution is a powerful tool to modify substrate specificity for a wide array of enzyme catalysts. In this issue of Chemistry & Biology, Thorson and coworkers use directed evolution to increase the catalytic proficiency of a model glycosyltransferase, OleD, 300-fold for a nonphysiological substrate (Williams et al., 2008).
authors.affiliation: College of Pharmacy and Department of Chemistry, Dalhousie University, Halifax, Nova Scotia B3H 3J5, Canada. david.jakeman@dal.ca
authors.forename: David L
authors.initials: DL
authors.lastname: Jakeman
mesh_terms: D019943:Amino Acid Substitution; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D019020:Directed Molecular Evolution / Q000379:methods*; D006031:Glycosylation; D016695:Glycosyltransferases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D009675:Novobiocin / Q000378:metabolism; D009827:Oleandomycin / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D009675:Novobiocin; D016695:Glycosyltransferases; D009827:Oleandomycin