Fast and efficient synthesis of a novel homologous series of L-fucosylated trisaccharides using the Helix pomatia alpha-(1-->2)-L-galactosyltransferase.
The alpha-(1-->2)-L-galactosyltransferase from the albumen gland of the vineyard snail Helix pomatia exhibits high alpha-(1-->2)-L-fucosyltransferase activity and can be used to transfer L-fucose from GDP-L-fucose to terminal, non-reducing D-galactose residues of an oligosaccharide, thus providing facile access to a range of H-antigen-containing oligosaccharides. The enzymatic glycosylation was applied here on a milligram scale to a series of disaccharide acceptor substrates. Apparently the site of interglycosidic linkage between the terminal and subterminal acceptor sugar units is of little or no consequence. The homologous series of trisaccharides thus produced were fully characterised by NMR analysis of their peracetates.
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002855:Chromatography, Thin Layer; D005643:Fucose / Q000378:metabolism; D005700:Galactosyltransferases / Q000378:metabolism*; D006372:Helix, Snails / Q000201:enzymology*; D008969:Molecular Sequence Data; D013379:Substrate Specificity; D014312:Trisaccharides / Q000138:chemical synthesis*
D014312:Trisaccharides; D005643:Fucose; D005700:Galactosyltransferases