title: Recent structures, evolution and mechanisms of glycosyltransferases.
abstract: Cellular glycome assembly requires the coordinated action of a large number of glycosyltransferases that catalyse the transfer of a sugar residue from a donor to specific acceptor molecules. This enzyme family is very ancient, encompassing all three domains of life. There has been considerable recent progress in structural glycobiology with the determination of crystal structures of several important glycosyltransferase members, showing novel folds and variations around a common α/β scaffold. Structural, kinetic and inhibitor data have led to the emergence of various scenarios with respect to their evolutionary history and reaction mechanisms thus highlighting the different solutions that nature has selected to catalyse glycosyl transfer.
authors: CERMAV-CNRS, University of Grenoble 1, BP 53, 38041 Grenoble, France. breton@cermav.cnrs.fr
authors: Christelle
authors: C
authors: Breton
authors: Sylvie
authors: S
authors: Fournel-Gigleux
authors: Monica M
authors: MM
authors: Palcic
mesh_terms: D055808:Drug Discovery; D004791:Enzyme Inhibitors / Q000494:pharmacology; D019143:Evolution, Molecular; D006025:Glycosaminoglycans / Q000096:biosynthesis; D016695:Glycosyltransferases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans
chemical_list: D004791:Enzyme Inhibitors; D006025:Glycosaminoglycans; D016695:Glycosyltransferases