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Characterization of a core α1→3‐fucosyltransferase from the snail Lymnaea stagnalis that is involved in the synthesis of complex‐type N ‐glycans
Author(s) -
van Tetering Angelique,
Schiphorst Wietske E.C.M,
van den Eijnden Dirk H,
van Die Irma
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01489-1
Subject(s) - fucosylation , lymnaea stagnalis , fucosyltransferase , biochemistry , snail , glycopeptide , asparagine , glycoprotein , glycan , biology , chemistry , enzyme , ecology , antibiotics
We have identified a core α1→3‐fucosyltransferase activity in the albumin and prostate glands of the snail Lymnaea stagnalis . Incubation of albumin gland extracts with GDP‐[ 14 C]Fuc and asialo/agalacto‐glycopeptides from human fibrinogen resulted in a labeled product in 50% yield. Analysis of the product by 400 MHz 1 H‐NMR spectroscopy showed the presence of a Fuc residue α1→3‐linked to the Asn‐linked GlcNAc. Therefore, the enzyme can be identified as a GDP‐Fuc:GlcNAc (Asn‐linked) α1→3‐fucosyltransferase. The enzyme acts efficiently on asialo/agalacto‐glycopeptides from both human fibrinogen and core α1→6‐fucosylated human IgG, whereas bisected asialo/agalacto‐glycopeptide could not serve as an acceptor. We propose that the enzyme functions in the synthesis of core α1→3‐fucosylated complex‐type glycans in L. stagnalis . Core α1→3‐fucosylation of the asparagine‐linked GlcNAc of plant‐ and insect‐derived glycoproteins is often associated with the allergenicity of such glycoproteins. Since allergic reactions have been reported after consumption of snails, the demonstration of core α1→3‐fucosylation in L. stagnalis may be clinically relevant.