InterPro domain: IPR038577

Glycosyltransferase family 10 ( GT10 ) comprises enzymes with two known activities; galactoside 3(4)-L-fucosyltransferase ( 2.4.1.65 ) and galactoside 3-fucosyltransferase ( 2.4.1.152 ).

The galactoside 3-fucosyltransferases display similarities with the alpha-2 and alpha-6-fucosyltranferases [ 1 ]. The biosynthesis of the carbohydrate antigen sialyl Lewis X (sLe(x)) is dependent on the activity of an galactoside 3-fucosyltransferase. This enzyme catalyses the transfer of fucose from GDP-beta-fucose to the 3-OH of N-acetylglucosamine present in lactosamine acceptors [ 2 ].

Some of the proteins in this group are responsible for the molecular basis of the blood group antigens, surface markers on the outside of the red blood cell membrane. Most of these markers are proteins, but some are carbohydrates attached to lipids or proteins [Reid M.E., Lomas-Francis C. The Blood Group Antigen FactsBook Academic Press, London / San Diego, (1997)]. Galactoside 3(4)-L-fucosyltransferase ( 2.4.1.65 ) belongs to the Lewis blood group system and is associated with Le(a/b) antigen.

Structural domains comprising this superfamily share the structure of the C-terminal domain of Glycosyltransferase family 10 (GT10). The C-terminal domain plays an important role in acceptor binding and specificity [ 3 ].

1. Conserved structural features in eukaryotic and prokaryotic fucosyltransferases. Glycobiology 8, 87-94
2. Chemical modification of an alpha 3-fucosyltransferase; definition of amino acid residues essential for enzyme activity. Biochim. Biophys. Acta 1334, 57-64
3. C-terminal amino acids of Helicobacter pylori alpha1,3/4 fucosyltransferases determine type I and type II transfer. J Biol Chem 278, 21893-900