Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 13, Issue 5-6, Pages 592-600Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.cbpa.2009.08.014
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Funding
- National Institutes of Health [R01 GM080374]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM080374] Funding Source: NIH RePORTER
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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.
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