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Updated: May 20, 2026

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
Recent structures, evolution and mechanisms of glycosyltransferases
Christelle Breton1, Sylvie Fournel-Gigleux, Monica M Palcic
1CERMAV-CNRS, University of Grenoble 1, BP 53, 38041 Grenoble, France. breton@cermav.cnrs.fr
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.
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