Strict order of (Fuc to Asn-linked GlcNAc) fucosyltransferases forming core-difucosylated structures.
In insect cells fucose can be either alpha1,6- or alpha1,3-linked to the asparagine-bound GlcNAc residue of N-glycans. Difucosylated glycans have also been found. Kinetic studies and acceptor competition experiments demonstrate that two different enzymes are responsible for this alpha1,6- and alpha1,3-linkage of fucose. Using dansylated acceptor substrates a strict order of these enzymes can be established for the formation of difucosylated structures. First, the alpha1,6-fucosyltransferase catalyses the transfer of fucose into alpha1,6-linkage to the non-fucosylated acceptor and then the alpha1,3-fucosyltransferase completes the difucosylation.
Staudacher
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Institut für Chemie, Universität für Bodenkultur, Vienna, Austria. estaud@edv2.boku.ac.at
März
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D000818:Animals; D001667:Binding, Competitive; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002460:Cell Line; D005643:Fucose / Q000737:chemistry / Q000378:metabolism*; D005647:Fucosyltransferases / Q000378:metabolism*; D006020:Glycopeptides / Q000096:biosynthesis* / Q000737:chemistry; D007700:Kinetics; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D018411:Spodoptera
D006020:Glycopeptides; D011134:Polysaccharides; D005643:Fucose; D005647:Fucosyltransferases