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A novel plant α4‐fucosyltransferase ( Vaccinium myrtillus L.) synthesises the Lewis a adhesion determinant
Author(s) -
Palma Angelina S.,
Vila-Verde Cidália,
Pires Ana Sofia,
Fevereiro Pedro S.,
Costa Júlia
Publication year - 2001
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(01)02568-6
Subject(s) - fucosyltransferase , chemistry , vaccinium myrtillus , stereochemistry , biochemistry , glycosylation , enzyme , fucose , fucosylation , residue (chemistry) , glycoprotein , botany , biology
We have partially characterised an α4‐fucosyltransferase (α4‐FucT) from Vaccinium myrtillus , which catalysed the biosynthesis of the Lewis a adhesion determinant. The enzyme was stable up to 50°C. The optimum pH was 7.0, both in the presence and in the absence of Mn 2+ . The enzyme was inhibited by Mn 2+ and Co 2+ , and showed resistance towards inhibition with N ‐ethylmaleimide. It transferred fucose to N ‐acetylglucosamine in the type I Galβ3GlcNAc motif from oligosaccharides linked to a hydrophobic tail and glycoproteins (containing the type I motif). Sialylated oligosaccharides containing the type II Galβ4GlcNAc motif were not acceptors. The catalytic mechanism of the plant α4‐FucT possibly involves a His residue, and it must have arisen by convergent evolution relative to its mammalian counterparts.