A novel plant α4‐fucosyltransferase (Vaccinium myrtillus L.) synthesises the Lewisa adhesion determinant

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Abstract
We have partially characterised an α4‐fucosyltransferase (α4‐FucT) from Vaccinium myrtillus, which catalysed the biosynthesis of the Lewisa 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 Mn2+. The enzyme was inhibited by Mn2+ and Co2+, 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.