1998European Journal of Organic ChemistryRequires access

Regioselective Fucosylation Using L-Galactosyltransferase fromHelix pomatia

Laurent F. Bornaghi, Lisa Keating, Hayley M. Binch, Hagen Bretting, Joachim Thiem

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Abstract

The L-galactosyltransferase from Helixpomatia catalyses the transfer of L-galactose from GDP-L-galactose to various disaccharides having a D-galactose at the non-reducing position, forming an α(1→2) linkage. L-Fucose, an important part of the human blood determinant, is also transferred by this enzyme, allowing the formation of H-blood group determinant. The transfer of L-fucose has been studied with four disaccharides: the Galβ(1→3)GalβOMe, the Galβ(1→3)GalNAcαOThr, the Galβ(1→3)GalαOMe, and the Galβ(1→3)GlcNAcβOMe.

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What this paper is about

The L-galactosyltransferase from Helixpomatia catalyses the transfer of L-galactose from GDP-L-galactose to various disaccharides having a D-galactose at the non-reducing position, forming an α(1→2) linkage. L-Fucose, an important part of the human blood determinant, is also transferred by this enzyme, allowing the formation of H-blood group determinant. The transfer of L-fucose has been studied with four disaccharides: the Galβ(1→3)GalβOMe, the Galβ(1→3)GalNAcαOThr, the Galβ(1→3)GalαOMe, and the Galβ(1→3)GlcNAcβOMe.

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Available abstract

The L-galactosyltransferase from Helixpomatia catalyses the transfer of L-galactose from GDP-L-galactose to various disaccharides having a D-galactose at the non-reducing position, forming an α(1→2) linkage. L-Fucose, an important part of the human blood determinant, is also transferred by this enzyme, allowing the formation of H-blood group determinant. The transfer of L-fucose has been studied with four disaccharides: the Galβ(1→3)GalβOMe, the Galβ(1→3)GalNAcαOThr, the Galβ(1→3)GalαOMe, and the Galβ(1→3)GlcNAcβOMe.

Key concepts: Fucosylation, Chemistry, Galactosyltransferase, Fucose, Galactose, Glycoconjugate, Fucosidase, Stereochemistry

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