Transglycosylases

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• Author: Spencer Williams
• Responsible Curator: Spencer Williams

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Overview

Transglycosylases are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the interchange of an aglycon of a glycoside. Mechanistically, transglycosylases utilize the same mechanism as certain retaining glycoside hydrolases. Thus, reaction of the glycoside hydrolase with a substrate gives a glycosyl-enzyme intermediate that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide [1]. Some transglycosidases possess substantial glycoside hydrolase activity, and some glycoside hydrolases possess transglycosylases activity. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are classified as glycoside hydrolases into various GH families on the basis of sequence similarity.

Generalized mechanism of a transglycosylase. Enzymatic cleavage of a substrate through a classical retaining mechanism results in formation of a glycosyl enzyme intermediate. This can partition to react with either water to cause hydrolysis (glycoside hydrolase activity) or to an alternative acceptor, often a sugar, to cause transglycosylation (transglycosylase activity).

References

1. Crout DH and Vic G. (1998). Glycosidases and glycosyl transferases in glycoside and oligosaccharide synthesis. Curr Opin Chem Biol. 1998;2(1):98-111. DOI:10.1016/s1367-5931(98)80041-0 |