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Tandem Exploitation of Helix pomatia Glycosyltransferases: Facile Syntheses of H‐Antigen‐Bearing Oligosaccharides
Author(s) -
Bretting Hagen,
Buck Friedrich,
Jacobs Günter,
Meinke Sebastian,
Scheppokat Angela M.,
Thiem Joachim
Publication year - 2007
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200700440
Subject(s) - glycosyltransferase , chemistry , stereochemistry , helix pomatia , acceptor , transferase , disaccharide , biochemistry , galactose , enzyme , biology , snail , physics , condensed matter physics , ecology
Snails from the family Helicidae produce in their albumen glands a highly branched galactan, which consists almost exclusively of D ‐ and L ‐galactose. The D ‐Gal residues are glycosydically β(1→6)‐ or β(1→3)‐linked, whereas the L ‐Gal moieties are attached α(1→2). Up until the present time, two β(1→6)‐ D ‐galactosyl transferases and one α(1→2)‐ L ‐galactosyl transferase have been identified in a membrane preparation of these glands. These were used to synthesise various oligosaccharides by successive addition of the NDP‐activated (NDP=nucleoside‐5′‐diphosphate) D ‐Gal or L ‐Fuc moieties, up to a heptasaccharide by starting from the disaccharide D ‐Gal‐β(1→3)‐ D ‐Gal‐β(1→OMe. Even larger oligosaccharides up to a tridecasaccharide were obtained by starting with the hexasaccharide D ‐Gal‐[β(1→3)‐ D ‐Gal] 4 ‐β(1→4)‐ D ‐Glc as an acceptor substrate. This tandem exploitation process has high potential for the easy introduction of D ‐Gal and L ‐Fuc residues into a great variety of oligosaccharides, which can be used in ligand/acceptor studies.