Glycosyltransferases
Glycosyltransferases are a type of enzyme that catalyze the formation of glycosidic linkages through the transfer of monosaccharides from a sugar nucleotide to a receiving molecule, often another saccharide. Find out more about glycosyltransferase enzymes below and uncover strategies to prevent glycotransferase inhibition plus products to assist your research.
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Glycosyltransferase Enzymes and Reagents
Glycosyltransferases are specific for the type of linkage (α or β), and the linkage position of the glycoside bond formed [e.g. α(1→3) or β(1→4)]. Glycosyltransferases were initially considered to be specific for a single glycosyl donor and acceptor, which led to the “one enzyme-one linkage” concept.1,2 Subsequent observations have refuted the theory of absolute enzymatic specificity by describing the transfer of analogs of some nucleoside mono- or diphosphate sugar donors.3‑8
Glycosyltransferases can tolerate modifications to the acceptor sugar, as long as the acceptor meets specific structural requirements, e.g., appropriate stereochemistry and availability of the reactive hydroxyl group involved in the glycosidic bond.
In contrast to organic chemical synthesis, enzymatic glycosylation has potential for application use within biological systems, where the modification of glycosylation sites may be used to investigate the regulation of cell signaling processes. Various application strategies for glycosyltransferases have employed an assortment of glycosyl donors and reaction conditions for the synthesis of carbohydrates and the glycosylation of natural products.9,10
A major limitation to enzyme-catalyzed glycosylation reactions is the glycosyltransferase inhibition caused by nucleotide diphosphates generated during the reaction. Two strategies have been identified to prevent enzymatic inhibition (Figure 1):
- Phosphatase is added to the reaction to degrade the nucleotide diphosphates by removal of the phosphate group (Figure 1A).11
- Nucleotide diphosphates are recycled to the appropriate nucleotide triphosphates by employing multi-enzyme regeneration schemes. Although several different enzymes and cofactors are involved in these in situ regeneration schemes, the method avoids the use of stoichiometric amounts of sugar nucleotides (Figure 1B).12‑14
Figure 1.Methods for avoiding enzyme inhibition in glycosyltransferase-catalyzed synthesis. (A) Addition of phosphatase. (B) Recycling of sugar nucleotides (NDP = nucleotide diphosphates, NTP = nucleotide triphosphates, N = nucleotide, Pi = phosphate).
Syntheses of drug-sugar conjugates derived from the broad range of naturally occurring glycosides underscore the potential of using glycosylated pharmaceuticals in drug delivery, where the sugar moiety may increase the solubility and bioavailability of large hydrophobic molecules under mild conditions.15-19
Preparative Use
We have developed recombinant and native glycosyltransferases and sugar nucleotides for preparative carbohydrate synthesis and directed modification of carbohydrate moieties. The great advantage of enzymatic synthesis is that the enzymes tend to be regio- and stereo- specific, forgoing the need for blocking and complicated branching carbohydrate organic chemistry. Our glycosyltransferases combined with the appropriate nucleotide sugar donor can be used for transfer of a specific monosaccharide moiety to an acceptor substrate on a small preparative scale.
- Unique glycosyltransferases—deliver regiospecific and stereospecific glycosylation
- Individual enzyme aliquots for each glycosylation reaction—prevent enzyme activity loss and cross-contamination
Glycosyltransferases and nucleotide sugar donors are available separately*.
Each kit is sufficient for 5 glycosylation reactions.
*Sales restrictions may apply. Please contact your local sales representative.
Find more technical resources on our Glycobiology hub page.
References
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