title: Enzymatic transglycosylation for glycoconjugate synthesis.
abstract: Remarkable advances have been made in recent years in exploiting the transglycosylation activity of glycosidases and glycosynthase mutants for oligosaccharide and glycoconjugate synthesis. New glycosynthases were generated from retaining glycosidases, inverting glycosidases, and those that proceed in a mechanism of substrate-assisted catalysis. Directed evolution coupled with elegant screening methods has led to the discovery of an expanding number of glycosynthase mutants that show improved catalytic activity and/or altered substrate specificity. In particular, enzymatic transglycosylation strategy has been recently extended to the synthesis of complex glycoconjugates, including glycosphingolipids, N-glycoproteins, and other glycosylated natural products.
authors.affiliation: Institute of Human Virology and Department of Biochemistry & Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. LWang3@ihv.umaryland.edu
authors.forename: Lai-Xi
authors.initials: LX
authors.lastname: Wang
authors.forename: Wei
authors.initials: W
authors.lastname: Huang
mesh_terms: D055162:Biocatalysis; D001688:Biological Products / Q000096:biosynthesis / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D006001:Glycoconjugates / Q000096:biosynthesis* / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D006027:Glycosides / Q000378:metabolism; D006031:Glycosylation; D006801:Humans
chemical_list: D001688:Biological Products; D004798:Enzymes; D006001:Glycoconjugates; D006027:Glycosides; D006026:Glycoside Hydrolases; C050427:endoglycoceramidase