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Conversion of GalNAcβ(1–4)GlcNAcβ‐OMe into GalNAcβ(1–4)‐[Fucα(1–3)]GlcNAcβ‐OMe using human milk α3/4‐fucosyltransferase synthesis of a novel terminal element in glycoprotein glycans
Author(s) -
Bergwerff Aldert A.,
van Kuik J.Albert,
Schiphorst Wietske E.C.M.,
Koeleman Carolien A.M.,
van den Eijnden Dirk H.,
Kamerling Johannis P.,
Vliegenthart Johannes F.G.
Publication year - 1993
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 - 10.1016/0014-5793(93)81698-y
Subject(s) - fucosyltransferase , fucosylation , chemistry , glycan , stereochemistry , substituent , fucose , biochemistry , glycoprotein , enzyme
Incubation of GalNAcβ(1–4)GlcNAcβ‐OMe with GDP‐Fuc in the presence of human milk α3/4‐fucosyltransferase resulted in the formation of GalNAcβ(1–4)[Fucα(1–3)]GlcNAcβ‐OMe. Under conditions that led to complete α3‐fucosylation of Galβ(1–4)GlcNAcβ‐OEt, GalNAcβ(1–4)GlcNAcβ‐OMe was fucosylated for more than 85%. For the identification of the isolated fucosylated products one‐ and two‐ dimensional 1 H‐NMR spectroscopy was applied. In vacuo molecular dynamics simulations of Galβ(1–4)[Fucα(1–3)]GlcNAcβ‐OEt and GalNAcβ(1–4)[Fucα(1–3)]GlcNAcβ‐OMe using the CHARMm based force field CHEAT, demonstrated only small differences between the conformations of these compounds. This illustrates the minor conformational influence of the substituent at C‐2′, i.e. a hydroxyl function versus a N ‐acetyl group.