This is an abbreviated version! For detailed information about 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase, go to the full flat file.
the last step in sLex epitope formation is catalyzed byalpha(1,3)-fucosyltransferase VII, i.e. FucTVII, which transfers a fucosyl moiety from GDP-fucose to the core oligosaccharide structures, overview
the gene is capable of directing expression of the Lewis x Galbeta(1,4)(Fucalpha(1,3))GlcNAc, sialyl Lewis x NeuNAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAc, and difucosyl sialyl Lewis x NeuNAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAc epitopes
the gene is capable of directing expression of the Lewis x Galbeta(1,4)(Fucalpha(1,3))GlcNAc, sialyl Lewis x NeuNAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAc, and difucosyl sialyl Lewis x NeuNAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAc epitopes
the enzyme is involved in the biosynthesis of the E-selectin ligand, sialyl-Lewis X. Catalyzes the transfer of fucose from GDP-beta-fucose to alpha-2,3 sialylated substrates
the enzyme is involved in the biosynthesis of the E-selectin ligand, sialyl-Lewis X. Catalyzes the transfer of fucose from GDP-beta-fucose to alpha-2,3 sialylated substrates
the enzyme is involved in the biosynthesis of the E-selectin ligand, sialyl-Lewis X. Catalyzes the transfer of fucose from GDP-beta-fucose to alpha-2,3 sialylated substrates
the enzyme is involved in the biosynthesis of the E-selectin ligand, sialyl-Lewis X. Catalyzes the transfer of fucose from GDP-beta-fucose to alpha-2,3 sialylated substrates
FucT-VI is involved in the biosynthesis of nonsialylated Lewis X, i.e. Lex, antigen, FucT VII is essential for biosynthesis of the carbohydrate antigen sialyl Lewis X, i.e. sLex, in leukocytes, FucT VII and FucT IV are essential for biosynthesis of selectin binding ligands in T-cells
the alpha3-fucosyltransferase IX, FUT9, catalyses the transfer of fucose in an alpha3 linkage onto terminal type II Galbeta4GlcNAc acceptors, the final step in the biosynthesis of the Lewisx epitope, in neurons, overview
the alpha3-fucosyltransferase IX, FUT9, catalyses the transfer of fucose in an alpha3 linkage onto terminal type II Galbeta4GlcNAc acceptors, the final step in the biosynthesis of the Lewisx epitope, in neurons, overview
the final step in the biosynthesis of Lex is catalyzed by alpha3-fucosyltransferases with different specificites, which add a fucose residue to type II-based oligosaccharide chains, the alpha3-FUT activity in NT2 cells is the result of combined activities of FUT4 ad FUT9 whereas in NT2N cells only FUT9 participatein the Lex biosynthesis, overview
the final step in the biosynthesis of Lex is catalyzed by alpha3-fucosyltransferases with different specificites, which add a fucose residue to type II-based oligosaccharide chains, the alpha3-FUT activity in NT2 cells is the result of combined activities of FUT4 ad FUT9 whereas in NT2N cells only FUT9 participatein the Lex biosynthesis, overview
the natural substrate of FucTVII is a glycoprotein carrying 3'SLN-terminated polylactoseamine chains, FucTVII activity is required for synthesis of the sialyl-Lewis X glycoepitopes on the E- and P-selectin ligands, necessary for lymphocyte migration into the skin
Fuc-TVII participates in the generation of alpha(1,3)fucosylated ligands for L-selectin, evidence for a role for this enzyme in E- and P-selectin ligand expression in leukocytes