Abstract
Enzymes are nature’s catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.
Highlights
Enzymes were already used for the conversion of glycosides even before all stereochemical details of the known carbohydrates were assigned [1,2]
As Leloir glycosyltransferases use the elimination of the nucleotide as a driving force for the glycosylation reaction, the high energy gain poses a problem during the regeneration of nucleotide diphosphate (NDP)-sugar donors
The discovery, characterization, and engineering of Leloir glycosyltransferases has expanded the synthetic toolbox to couple, elongate, or branch glycoconjugates, oligosaccharides, and glycans with high regio- and stereoselectivity
Summary
Luuk Mestrom 1 , Marta Przypis 2,3 , Daria Kowalczykiewicz 2,3 , André Pollender 4 , Antje Kumpf 4,5 , Stefan R. Microbial Biotechnology, Faculty of Biology & Biotechnology, Ruhr-Universität Bochum, Universitätsstr. 150, 44780 Bochum, Germany
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