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Regioselective Fucosylation Using L-Galactosyltransferase from Helix pomatia

✍ Scribed by Laurent Bornaghi; Lisa Keating; Hayley Binch; Hagen Bretting; Joachim Thiem

Book ID
101277274
Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
197 KB
Volume
1998
Category
Article
ISSN
1434-193X

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✦ Synopsis

The L-galactosyltransferase from Helix pomatia catalyses the this enzyme, allowing the formation of H-blood group determinant. The transfer of L-fucose has been studied with transfer of L-galactose from GDP-L-galactose to various disaccharides having a D-galactose at the non-reducing four disaccharides: the Galβ(1Ǟ3)GalβOMe, the Galβ(1Ǟ3)-GalNAcαOThr, the Galβ(1Ǟ3)GalαOMe, and the Galβ-position, forming an α(1Ǟ2) linkage. L-Fucose, an important part of the human blood determinant, is also transferred by (1Ǟ3)GlcNAcβOMe.

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✍ Angela Michelle Scheppokat; Minoru Morita; Joachim Thiem; Hagen Bretting 📂 Article 📅 2003 🏛 Elsevier Science 🌐 English ⚖ 213 KB

The a(12)-L-galactosyltransferase from Helix pomatia transfers an L-fucosyl residue from GDP-L-Fucose to a terminal, non-reducing D-galactopyranosyl moiety of an oligosaccharide. The extent of the enzyme's specificity towards the stereochemistry at the D-galactopyranosyl anomeric centre, the site of