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Regioselective Fucosylation Using L‐Galactosyltransferase from Helix pomatia
Author(s) -
Bornaghi Laurent,
Keating Lisa,
Binch Hayley,
Bretting Hagen,
Thiem Joachim
Publication year - 1998
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/(sici)1099-0690(199811)1998:11<2493::aid-ejoc2493>3.0.co;2-k
Subject(s) - fucosylation , chemistry , galactosyltransferase , fucose , galactose , glycoconjugate , fucosidase , stereochemistry , fucosyltransferase , biochemistry , regioselectivity , enzyme , catalysis
The L‐galactosyltransferase from Helix pomatia 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.