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Enzymatic route to preparative-scale synthesis of UDP-GlcNAc/GalNAc, their analogues and GDP-fucose.

Authors
Type
Published Article
Journal
Nature protocols
Publication Date
Volume
5
Issue
4
Pages
636–646
Identifiers
DOI: 10.1038/nprot.2010.3
PMID: 20224564
Source
Medline

Abstract

Enzymatic synthesis using glycosyltransferases is a powerful approach to building polysaccharides with high efficiency and selectivity. Sugar nucleotides are fundamental donor molecules in enzymatic glycosylation reactions by Leloir-type glycosyltransferases. The applications of these donors are restricted by their limited availability. In this protocol, N-acetylglucosamine (GlcNAc)/N-acetylgalactosamine (GalNAc) are phosphorylated by N-acetylhexosamine 1-kinase (NahK) and subsequently pyrophosphorylated by N-acetylglucosamine uridyltransferase (GlmU) to give UDP-GlcNAc/GalNAc. Other UDP-GlcNAc/GalNAc analogues can also be prepared depending on the tolerance of these enzymes to the modified sugar substrates. Starting from L-fucose, GDP-fucose is constructed by one bifunctional enzyme L-fucose pyrophosphorylase (FKP) via two reactions.

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