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6-deoxy-6-N-(2-naphthalene-2-yl-acetamide)-beta-L-galactopyranos-1-yl-guanosine 5'-diphosphate + sialyl-alpha-2,3-LacNAc-O-(CH2)3-N-dansyl
GDP + Galbeta(1-4)-[6-deoxy-6-N-(2-naphthalene-2-yl-acetamide)-L-Galbeta(1-3)]GlcNAc-O-(CH2)3-N-dansyl
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Substrates: via intermediate 6-azid0-1,2,3,4-tetra-O-benzoyl-6-deoxy-beta-L-galactopyranose, 6-deoxy-6-N-(2-naphalene-2-yl-acetamide)-beta-L-galactopyranos-1-yl-guanosine 5'-diphosphate disodium salt is the most sensitive and selective donor substrate for FUT-VI among all of the GDP-Fuc analogues, including the parent GDP-Fuc, known to date
Products: -
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6-deoxy-6-N-(2-naphthalene-2-yl-acetamide)-beta-L-galactopyranos-1-yl-guanosine 5'-diphosphate disodium salt + dansylated sialyl-alpha2,3-LacNAc
sLex tetrasaccharide
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Substrates: -
Products: -
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GDP-6,7-dideoxy-beta-L-galacto-hept-6-enopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl 6,7-dideoxy-beta-L-galacto-hept-6-enopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
Substrates: -
Products: -
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GDP-6-azido-6-deoxy-beta-L-galactopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl -6-azido-6-deoxy-beta-L-galactopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
Substrates: -
Products: -
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GDP-6-deoxy-6-fluoro-beta-L-galactopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl -6-deoxy-6-fluoro-beta-L-galactopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
Substrates: -
Products: -
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GDP-6-O-methyl-beta-L-galactopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl 6-O-methyl-beta-L-galactopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
Substrates: -
Products: -
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GDP-alpha-D-(5-cyano)arabinopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl alpha-D-(5-cyano)arabinopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
Substrates: -
Products: -
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GDP-alpha-D-arabinopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl alpha-D-arabinopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
Substrates: -
Products: -
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GDP-alpha-L-fucose + asialofetuin
GDP + ?
GDP-alpha-L-fucose + fetuin
GDP + ?
GDP-alpha-L-fucose + glycoprotein gp130
GDP + ?
GDP-beta-fucose + alpha2,3-sialyl N-acetyllactosamine
GDP + alpha1,3-fucosyl-alpha2,3-sialyl-N-acetyllactosamine
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Substrates: FucT-VII and FucT-IV
Products: -
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GDP-beta-fucose + alpha2,3-sialyl N-acetyllactosaminyl-R
GDP + alpha1,3-fucosyl-alpha2,3-sialyl-N-acetyllactosaminyl-R
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Substrates: FucT-VII and FucT-IV
Products: -
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GDP-beta-fucose + lacto-N-neotetraose
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc
Substrates: -
Products: -
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GDP-beta-fucose + lactose
GDP + alpha1,3-fucosyllactose
Substrates: N-acetyllactosamine is preferred over lactose
Products: -
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GDP-beta-fucose + N-acetyllactosamine
GDP + alpha1,3-fucosyl-N-acetyllactosamine
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc
?
GDP-beta-L-fucose + 4-deoxy-Galbeta1,4GlcNAc
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GDP-beta-L-fucose + alpha(2,3) bisialylated biantennary glycan
?
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Substrates: -
Products: -
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GDP-beta-L-fucose + asialo-erythropoietin
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Substrates: wild-type FUT9 efficiently fucosylates di-, tri- and tetraantennary N-glycans from asialoEPO
Products: -
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GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R
GDP + beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-R
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Substrates: -
Products: -
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GDP-beta-L-fucose + D-lactose
GDP + 3 L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-Glc
Substrates: the enzyme has very low relative substrate specificity toward D-lactose
Products: -
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GDP-beta-L-fucose + fetuin
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Substrates: -
Products: -
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GDP-beta-L-fucose + fetuin-biotin
?
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Substrates: -
Products: -
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GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
GDP-beta-L-fucose + Fucalpha1-2Galbeta1-4Glc
GDP + Fucalpha1-2Galbeta1-4Glcalpha1-3Fuc
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Substrates: -
Products: -
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GDP-beta-L-fucose + Galbeta1,4GlcNAc
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GDP-beta-L-fucose + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc
GDP + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glcalpha1-3Fuc
GDP-beta-L-fucose + Galbeta1-4Glc
GDP + Galbeta1-4Glcalpha1-3Fuc
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Substrates: -
Products: -
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GDP-beta-L-fucose + Galbeta1-4GlcNAcalpha-4-nitrophenol
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcalpha-4-nitrophenol
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Substrates: preferred substrate of CEFT-4 and CEFT-3
Products: -
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GDP-beta-L-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
GDP-beta-L-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
GDP-beta-L-fucose + lacto-N-neotetraose
GDP + lacto-N-fucopentaose III
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Substrates: -
Products: -
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GDP-beta-L-fucose + lactose
GDP + alpha1,3-fucosyllactose
Substrates: -
Products: -
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GDP-beta-L-fucose + N-acetyl-D-lactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
GDP-beta-L-fucose + N-acetyllactosamine
GDP + ?
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Substrates: -
Products: -
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GDP-beta-L-fucose + N-acetyllactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-6-O-sulfo-GlcNAc beta-O-C3H6-biotin
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Substrates: i.e. 6-sulfo-3'SLN, best substrate
Products: -
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GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-GlcNAc beta-(1,3)-Galbeta-(1,4)-Glcbeta-O-C3H6-biotin
?
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Substrates: i.e. 3'SLNL
Products: -
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GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-GlcNAc beta-O-BSA-biotin
?
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Substrates: i.e. 3'SLN-BSA
Products: -
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GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-GlcNAc beta-O-C3H6-biotin
?
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Substrates: i.e. 3'SLN
Products: -
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GDP-beta-L-fucose + Neu5Acalpha-(2,3)-Galbeta-(1,4)-GlcNAcbeta-R
GDP + Neu5Acalpha-(2,3)-Galbeta-(1,4)-[Fucalpha-(1,3)]-GlcNAcbeta-R
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Substrates: 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
Products: i.e. antigen sLex
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GDP-beta-L-fucose + NeuAcalpha(2,3)Galbeta(1,4)Glc
?
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Substrates: -
Products: -
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GDP-beta-L-fucose + NeuAcalpha2,3Galbeta1,4GlcNAc
?
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Substrates: 32% of the activity with Galbeta1,4GlcNAc
Products: -
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GDP-beta-L-fucose + NeuNAcalpha(2->3)Galbeta(1->4)GlcNAc
GDP + NeuNAcalpha(2->3)Galbeta(1->4)[L-Fucalpha(1->3)]GlcNAc
Substrates: best substrate
Products: -
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GDP-beta-L-fucose + octyl Galbeta(1->4)GlcNAc
GDP + octyl Galbeta(1->4)[L-Fucalpha(1->3)]GlcNAc
Substrates: -
Products: -
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GDP-beta-L-fucose + unsialylated biantennary glycan
?
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Substrates: -
Products: -
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GDP-beta-L-galactopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl beta-L-galactopyranosyl-(1->3)-[beta-D-galactopyranosyl-(1->4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
Substrates: -
Products: -
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GDP-fucose + (-3GalNAcbeta1-4GlcNAcbeta1-)n
GDP + (-3GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-)n
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Substrates: -
Products: N-glycans containing poly-LDN structures are efficiently fucosylated by human FucT9 producing poly-LDNF structures, max. 4-6 repeating LDNF units
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GDP-fucose + (Galbeta1-4Galbeta1-4GlcNAcbeta1-2Manalpha1-6[Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3])Manbeta1-4GlcNAc
GDP + (Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-6[Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3])Manbeta1-4GlcNAc
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Substrates: oligosaccharides are determined by a combination of exoglycosidase digestions and two-dimensional HPLC sugar mapping, most of these oligosaccharides are free form
Products: -
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GDP-fucose + (Galbeta1-4Galbeta1-4GlcNAcbeta1-2Manalpha1-6[Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3])Manbeta1-4GlcNAcbeta1-4GlcNAc
GDP + (Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-6[GalbetaGalbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3])Manbeta1-4GlcNAcbeta1-4GlcNAc
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Substrates: -
Products: -
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GDP-fucose + asialo human erythropoietin
GDP + fucosylated asialo human erythropoietin
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Substrates: -
Products: -
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GDP-fucose + bovine asialofetuin
GDP + fucosylated bovine asialofetuin
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Substrates: -
Products: -
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GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAc
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc
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Substrates: -
Products: -
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GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc-O-(CH2)3NHCO(CH2)5-biotin
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Substrates: -
Products: -
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GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAcbeta1-R
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-R
Substrates: -
Products: Lewis Y antigen, increased expression in cancer cells
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GDP-fucose + Galbeta(1,3)GlcNAcOMe
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcOMe
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Substrates: -
Products: -
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GDP-fucose + Galbeta1-4Glc
GDP + Galbeta1-4 (Fucalpha1-3)Glc
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Substrates: -
Products: -
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GDP-fucose + Galbeta1-4Glc-NAc-O-(CH2)3NHCO(CH2)5-NH-biotin
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
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Substrates: -
Products: -
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GDP-fucose + Galbeta1-4GlcNAc
GDP + Galbeta1-4 (Fucalpha1-3)GlcNAc
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Substrates: -
Products: -
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GDP-fucose + Galbeta1-4GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
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Substrates: sFUT9 efficiently fucosylates type II acceptors but not the corresponding sialylated acceptors, and only very poorly the type I (Galbeta3GlcNAc-R) related acceptors
Products: -
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GDP-fucose + Galbeta1-4GlcNAc-R
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-R
GDP-fucose + Galbeta1-4GlcNAcbeta1-2Manalpha1-6(Galbeta1-4GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-Asn
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-6(Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-Asn
Substrates: -
Products: -
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GDP-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-PA
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc-PA
Substrates: Lacto-N-neo-tetraose is a Lewis-type FucT substrate
Products: -
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GDP-fucose + GalNAcbeta1-4GlcNAcbeta-R
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-R
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Substrates: -
Products: -
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GDP-fucose + GalNAcbeta1-4GlcNAcbeta1-2Manalpha1-6(GalNAcbeta1-4GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-Asn
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-6(GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-Asn
Substrates: -
Products: -
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GDP-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + GalNAcbeta1-4[Fucalpha1-3]GlcNAcbeta1-3Galbeta1-4Glc
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Substrates: incubation with extracts from transfected COS7 cells
Products: product obtained at a level of about 50% of that obtained with the acceptor GalNAcbeta1-4GlcNAcbeta1-R
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GDP-fucose + GalNAcbeta1-4GlcNAcbeta1-R
GDP + GalNAcbeta1-4[Fucalpha1-3]GlcNAcbeta1-R
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Substrates: -
Products: -
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GDP-fucose + human erythropoietin
GDP + fucosylated human erythropoietin
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Substrates: -
Products: -
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GDP-fucose + LacNAc
GDP + ?
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Substrates: -
Products: -
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GDP-fucose + LacNAcbeta-O-(CH2)5CO2CH3
GDP + ?
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Substrates: -
Products: -
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GDP-fucose + lacto-N-neotetraose
GDP + ?
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Substrates: -
Products: -
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GDP-fucose + lacto-N-neotetraose
GDP + lacto-N-fucopentaose III
GDP-fucose + methyl beta-D-2-O-methylgalactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
GDP + methyl beta-D-2-O-methylgalactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-2-O-methylgalactosyl-(1-4)-6-O-methyl-N-acetyl-beta-D-glucosamine
GDP + methyl beta-D-2-O-methylgalactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-6-O-methyl-N-acetyl-beta-D-glucosamine
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-2-O-methylgalactosyl-(1-4)-N-acetyl-beta-D-glucosamine
GDP + methyl beta-D-2-O-methylgalactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-N-acetyl-beta-D-glucosamine
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-acetylamino-beta-D-glucopyranose
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-acetylamino-beta-D-glucopyranose
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-amino-beta-D-glucopyranose
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-amino-beta-D-glucopyranose
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-methylsulfonylamino-beta-D-glucopyranose
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-methylsulfonylamino-beta-D-glucopyranose
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl amide
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl amide
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl ester
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl ester
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-galactosyl-(1-4)-6-O-methyl-N-acetyl-beta-D-glucosamine
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-6-O-methyl-N-acetyl-beta-D-glucosamine
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Substrates: -
Products: -
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GDP-fucose + methyl beta-D-galactosyl-(1-4)-6-O-methylsulfonyl-N-acetyl-beta-D-glucosamine
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-6-O-methylsulfonyl-N-acetyl-beta-D-glucosamine
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Substrates: -
Products: -
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GDP-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc
GDP + NeuAcalpha2-3Galbeta1-4(Fucalpha1-3)GlcNAc
GDP-fucose + sialyl-alpha-2,3-N-acetyllactosamine
GDP + NeuNAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAc
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Substrates: -
Products: -
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GDP-L-fucose + 2'-fucosyllactose
GDP + ?
Substrates: 42% of the activity with Galbeta(1,4)GlcNAc
Products: -
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GDP-L-fucose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl 6-deoxy-beta-L-galactopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
Substrates: -
Products: -
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GDP-L-fucose + 3'-sialyl N-acetyl lactosamine
GDP + ?
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Substrates: -
Products: -
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GDP-L-fucose + alpha(2,3)-sialyllactosamine
GDP + ?
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Substrates: 115% of the activity with Galbeta(1,4)GlcNAc
Products: -
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GDP-L-fucose + alpha(2,3)sialyllactosamine
GDP + ?
Substrates: -
Products: -
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GDP-L-fucose + alpha1 acid glycoprotein
GDP + ?
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Substrates: with the major terminal structure on N-linked chains: NeuAc(2,3/6)Galbeta(1,4)GlcNAcbeta-R
Products: -
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GDP-L-fucose + asialo-alpha1-acid glycoprotein
GDP + ?
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Substrates: with the major terminal structure on N-linked chains: Galbeta(1,4)GlcNAcbeta-R
Products: -
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GDP-L-fucose + asialo-fetuin
GDP + ?
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Substrates: with the major terminal structure on N-linked chains: Galbeta(1,4)GlcNAcbeta-R
Products: -
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GDP-L-fucose + asialotransferrin
GDP + ?
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Substrates: -
Products: -
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GDP-L-fucose + desialylated alpha1-acid glycoprotein
GDP + ?
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Substrates: -
Products: -
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GDP-L-fucose + fetuin
GDP + ?
GDP-L-fucose + fetuin
GDP + alpha1,3-L-fucosyl-fetuin
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Substrates: FucT-VI
Products: -
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GDP-L-fucose + Fucalpha(1,2)Galbeta(1,3)GlcNAc-R
GDP + ?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)Glc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))Glc
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAcbeta(CH2)8COOMe
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(CH2)8COOMe
-
Substrates: -
Products: -
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAcbeta-bovine-serum-albumin
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta-bovine-serum-albumin
-
Substrates: -
Products: -
?
GDP-L-fucose + Galalpha(1,3)Galbeta(1,4)GlcNAc-R
GDP + ?
GDP-L-fucose + Galbeta(1,3)GlcNAc
GDP + ?
Substrates: i.e. lacto-N-biose I, 10% of the activity with Galbeta(1,4)GlcNAc
Products: -
?
GDP-L-fucose + Galbeta(1,4)-Glc
GDP + Galbeta(1,4)(Fucalpha(1,3))Glc
-
Substrates: 3% of the activity with Galbeta(1,4)GlcNAc
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
GDP-L-fucose + Galbeta(1,4)GlcNAc-O(CH2)8CO2CH3
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-O(CH2)8CO2CH3
GDP-L-fucose + Galbeta(1,4)GlcNAc-R
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-R
GDP-L-fucose + Galbeta(1,4)GlcNAcbeta(1,2)Manalpha(1,6)Manbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,2)Manalpha(1,6)Manbeta(1,4)GlcNAc
-
Substrates: -
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAcbeta(1,3)Galbeta(1,4)Glc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,3)Galbeta(1,4)Glc
-
Substrates: -
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAcbeta(1,3)Galbeta(1,4)Glc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,3)Galbeta(1,4)Glc + Galbeta(1,4)GlcNAcbeta(1,3)Galbeta(1,4)(Fucalpha(1,3))Glc
-
Substrates: -
Products: -
?
GDP-L-fucose + lacto-N-biose I
GDP + ?
Substrates: -
Products: -
?
GDP-L-fucose + lacto-N-fucopentaose I
GDP + ?
-
Substrates: -
Products: -
?
GDP-L-fucose + lacto-N-fucopentaose II
GDP + ?
-
Substrates: -
Products: -
?
GDP-L-fucose + lacto-N-tetraose
GDP + ?
-
Substrates: -
Products: -
?
GDP-L-fucose + lactose
GDP + ?
GDP-L-fucose + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-N-acetyl-beta-D-glucosaminyl]asparagine
GDP + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-[alpha-L-fucosyl-(1-3)]-N-acetyl-beta-D-glucosaminyl]asparagine
-
Substrates: -
Products: -
?
GDP-L-fucose + NeuAcalpha(2,3)Galbeta(1,4)GlcNAc
GDP + NeuAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
GDP-L-fucose + NeuAcalpha(2,3)Galbeta(1,4)GlcNAcbeta(1,2)Manalpha(1,6)Manbeta(1,4)GlcNAc
GDP + NeuAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,2)Manalpha(1,6)Manbeta(1,4)GlcNAc
-
Substrates: -
Products: -
?
GDP-L-fucose + sialyl-alpha-2,3-LacNAc-O-(CH2)3-N-dansyl
GDP + Galbeta(1-4)-[Fucalpha(1-3)]GlcNAc-O-(CH2)3-N-dansyl
-
Substrates: -
Products: -
?
GDP-L-fucose + sialyl-alpha-2,3-N-acetyllactosamine
GDP + NeuNAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAc
Substrates: -
Products: -
?
additional information
?
-
GDP-alpha-L-fucose + asialofetuin

GDP + ?
Substrates: -
Products: -
?
GDP-alpha-L-fucose + asialofetuin
GDP + ?
Substrates: -
Products: -
?
GDP-alpha-L-fucose + fetuin

GDP + ?
Substrates: -
Products: -
?
GDP-alpha-L-fucose + fetuin
GDP + ?
Substrates: -
Products: -
?
GDP-alpha-L-fucose + glycoprotein gp130

GDP + ?
Substrates: -
Products: -
?
GDP-alpha-L-fucose + glycoprotein gp130
GDP + ?
Substrates: -
Products: -
?
GDP-beta-fucose + N-acetyllactosamine

GDP + alpha1,3-fucosyl-N-acetyllactosamine
Substrates: N-acetyllactosamine is preferred over lactose. At a low GDP-fucose to acceptor ratio, the enzyme selectively fucosylates N-acetyllactosamine
Products: -
?
GDP-beta-fucose + N-acetyllactosamine
GDP + alpha1,3-fucosyl-N-acetyllactosamine
-
Substrates: FucT-VI
Products: -
?
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc

?
-
Substrates: 72% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc
?
-
Substrates: 135% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc
?
-
Substrates: 72% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc
?
-
Substrates: 72% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + 4-deoxy-Galbeta1,4GlcNAc

?
-
Substrates: 8% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + 4-deoxy-Galbeta1,4GlcNAc
?
-
Substrates: 8% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + 4-deoxy-Galbeta1,4GlcNAc
?
-
Substrates: 8% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc

?
-
Substrates: 99% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
-
Substrates: 115% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
-
Substrates: 99% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
-
Substrates: 99% of the activity with Galbeta1,4GlcNAc
Products: -
?
GDP-beta-L-fucose + Galbeta1,4GlcNAc

?
-
Substrates: -
Products: -
?
GDP-beta-L-fucose + Galbeta1,4GlcNAc
?
-
Substrates: -
Products: -
?
GDP-beta-L-fucose + Galbeta1,4GlcNAc
?
-
Substrates: -
Products: -
?
GDP-beta-L-fucose + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc

GDP + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glcalpha1-3Fuc
Substrates: -
Products: -
?
GDP-beta-L-fucose + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc
GDP + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glcalpha1-3Fuc
Substrates: -
Products: -
?
GDP-beta-L-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc

GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
-
Substrates: activity of CEFT-3 aqnd CEFT-4
Products: -
?
GDP-beta-L-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
-
Substrates: substrate of CEFT-3
Products: -
?
GDP-beta-L-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc

GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
-
Substrates: activity of CEFT-2
Products: -
?
GDP-beta-L-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
Substrates: activity of CEFT-2
Products: -
?
GDP-beta-L-fucose + N-acetyl-D-lactosamine

GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
Substrates: -
Products: -
?
GDP-beta-L-fucose + N-acetyl-D-lactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
Substrates: -
Products: -
?
GDP-beta-L-fucose + N-acetyllactosamine

GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
-
Substrates: -
Products: -
?
GDP-beta-L-fucose + N-acetyllactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
-
Substrates: -
Products: -
?
GDP-beta-L-fucose + N-acetyllactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
-
Substrates: -
Products: -
?
GDP-fucose + Galbeta1-4GlcNAc-R

GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-R
-
Substrates: -
Products: Lewis x determinant
?
GDP-fucose + Galbeta1-4GlcNAc-R
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-R
-
Substrates: -
Products: Lewis x determinant
?
GDP-fucose + lacto-N-neotetraose

GDP + lacto-N-fucopentaose III
-
Substrates: -
Products: -
?
GDP-fucose + lacto-N-neotetraose
GDP + lacto-N-fucopentaose III
-
Substrates: -
Products: -
?
GDP-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc

GDP + NeuAcalpha2-3Galbeta1-4(Fucalpha1-3)GlcNAc
-
Substrates: -
Products: sialyl Lewis x
?
GDP-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc
GDP + NeuAcalpha2-3Galbeta1-4(Fucalpha1-3)GlcNAc
-
Substrates: -
Products: -
?
GDP-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc
GDP + NeuAcalpha2-3Galbeta1-4(Fucalpha1-3)GlcNAc
-
Substrates: rate of reaction below 5% of the rate obtained toward nonsialylated acceptor
Products: sialyl Lewis x
?
GDP-L-fucose + fetuin

GDP + ?
-
Substrates: with the major terminal structure on N-linked chains: NeuAcalpha(2,3/6)Galbeta(1,4)GlcNAcbeta-R
Products: -
?
GDP-L-fucose + fetuin
GDP + ?
-
Substrates: -
Products: -
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,3)GlcNAc-R

GDP + ?
-
Substrates: -
Products: -
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,3)GlcNAc-R
GDP + ?
-
Substrates: -
Products: -
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)Glc

GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))Glc
-
Substrates: -
Products: -
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)Glc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))Glc
Substrates: -
Products: -
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)Glc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))Glc
-
Substrates: i.e. 2'-fucosyllactose, 17% of the activity with Galbeta(1,4)GlcNAc
Products: -
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAc

GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
Substrates: -
Products: -
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
Substrates: 162% of the activity with Galbeta(1,4)GlcNAc
Products: -
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
Substrates: mutant enzyme A349D shows 8fold higher activity than the wild-type enzyme
Products: -
?
GDP-L-fucose + Galalpha(1,3)Galbeta(1,4)GlcNAc-R

GDP + ?
-
Substrates: -
Products: -
?
GDP-L-fucose + Galalpha(1,3)Galbeta(1,4)GlcNAc-R
GDP + ?
-
Substrates: -
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAc

GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
Substrates: -
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
Substrates: i.e. N-acetyllactosamine
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
Substrates: i.e. N-acetyllactosamine
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
Substrates: i.e. N-acetyllactosamine
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAc-O(CH2)8CO2CH3

GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-O(CH2)8CO2CH3
-
Substrates: -
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAc-O(CH2)8CO2CH3
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-O(CH2)8CO2CH3
-
Substrates: -
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAc-R

GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-R
-
Substrates: -
Products: -
?
GDP-L-fucose + Galbeta(1,4)GlcNAc-R
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-R
-
Substrates: -
Products: -
?
GDP-L-fucose + lactose

GDP + ?
-
Substrates: -
Products: -
?
GDP-L-fucose + lactose
GDP + ?
-
Substrates: weak activity
Products: -
?
GDP-L-fucose + lactose
GDP + ?
Substrates: 11% of the activity with Galbeta(1,4)GlcNAc
Products: -
?
GDP-L-fucose + NeuAcalpha(2,3)Galbeta(1,4)GlcNAc

GDP + NeuAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
Substrates: -
Products: -
?
GDP-L-fucose + NeuAcalpha(2,3)Galbeta(1,4)GlcNAc
GDP + NeuAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
Substrates: 147% of the activity with Galbeta(1,4)GlcNAc
Products: -
?
additional information

?
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
Products: -
?
additional information
?
-
-
Substrates: -
Products: -
?
additional information
?
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Substrates: native enzyme utilizes only type 2 acceptors. Double mutation R115W/E116D slightly increases H-type 1 activity
Products: -
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additional information
?
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Substrates: no activity with Galbeta(1-3)GlcNAc-octyl, NeuAcalpha(2,3)Galbeta(1,3)GlcNAc and Fucalpha(1,2) Galalpha(1,4)GlcNAc
Products: -
?
additional information
?
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Substrates: no activity with Galbeta(1-3)GlcNAc-octyl, NeuAcalpha(2,3)Galbeta(1,3)GlcNAc and Fucalpha(1,2) Galalpha(1,4)GlcNAc
Products: -
?
additional information
?
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Substrates: the enzyme has acceptor specificity properties similar to that of the human myeloid enzyme FTIV
Products: -
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additional information
?
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Substrates: the recombinant enzyme has a clear preference for nonsialylated type-2 acceptors over either neutral type-1 acceptors or sialylated type-2 acceptors
Products: -
?
additional information
?
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Substrates: acceptor specificity of recombinant CEFTs, CEFT-1 acts on the N-glycan pentasaccharide core acceptor Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAcbeta1-Asn, while CEFT-2 does not, overview
Products: -
?
additional information
?
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
Products: -
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additional information
?
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
Products: -
?
additional information
?
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
Products: -
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additional information
?
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Substrates: the enzyme shows alpha1,3- and alpha1,4-fucosyltransferase activity
Products: -
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additional information
?
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Substrates: enzyme accepts fluorescein-isothiocyanate-labeled fucose and carboxyfluorescein-labeled fucose. Fluorescein-isothiocyanate-labeled NDP-beta-L-fucose is the best of these substrates
Products: -
?
additional information
?
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Substrates: the enzyme shows alpha1,3- and alpha1,4-fucosyltransferase activity
Products: -
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additional information
?
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Substrates: the enzyme shows alpha1,3- and alpha1,4-fucosyltransferase activity
Products: -
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additional information
?
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-
Substrates: -
Products: -
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additional information
?
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Substrates: catalyzes the transfer of the L-fucose moiety from guanosine diphosphate-beta-L-fucose to acceptor sugars to form biologically important fucoglycoconjugates, including sialyl Lewis x, the enzyme processes acceptor sugars with either oxygen or sulfur in the GlcNAc ring, but a similar sugar structure with nitrogen in the GlcNAc ring, is an inhibitor
Products: -
?
additional information
?
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Substrates: lactose and its fucose-substituted derivative are very poor acceptors for the enzyme
Products: -
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additional information
?
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-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: -
Products: -
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additional information
?
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Substrates: acceptor: type 2 H-oligosaccharide 8-methoxycarbonyloctyl glycoside
Products: -
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additional information
?
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Substrates: weak activity with type 1 substrates
Products: -
?
additional information
?
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Substrates: acceptor specificity with glycoprotein and glycolipid acceptors
Products: -
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additional information
?
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Substrates: fetuin and asialofetuin bearing N-linked carbohydrate chains containing the type II lactosamine core (Galbeta(1,4)GlcNAc)
Products: -
?
additional information
?
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Substrates: predominantly activity with sialylated or nonsialylated type-2 chain acceptors, only a low alpha(1,4)-fucosyltransferase activity with type-1 chain acceptors
Products: -
?
additional information
?
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Substrates: no activity with Galbeta(1,3)GlcNAc, NeuAcalpha2,6Galbeta(1,4)GlcNAc, NeuAcalpha2,8NeuAc and NeuAcalpha2,6Galbeta(1,4)Glc
Products: -
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additional information
?
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Substrates: enzyme utilizes only type-2 chain polylactosamines as substrates, sialylated and nonsialylated oligosaccharides are good substrates, the enzyme produces sialyl Lewis X and Lewis X determinants
Products: -
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additional information
?
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Substrates: the enzyme is active on the polylactosamine substrate having 6-sulfate modification at the GlcNAc moiety and gives rise to sialyl and nonsialyl 6-sulfo Lewis X. The enzyme is also active on alpha(1,2) fucosylated type 2 chain substrates
Products: -
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additional information
?
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Substrates: enzyme is involved in the expression of the sialyl-LewisX determinant, a ligand for E- and P-selectin
Products: -
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additional information
?
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Substrates: the hepatocellular enzyme is involved in the synthesis of sialosyl LeX determinants on cirrhotic alpha1AGP
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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
Products: -
?
additional information
?
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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
Products: -
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additional information
?
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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
Products: -
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additional information
?
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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
Products: -
?
additional information
?
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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
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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
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Substrates: assay development utilizing anion exchange chromatography
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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Substrates: 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
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Substrates: recombinant alpha1,3FucT-VII acts as a potential antiapoptotic factor in H7721 cells after induction of apoptosis by UV irradiation, overview
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Substrates: 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
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Substrates: 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
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Substrates: 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
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Substrates: 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
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Substrates: FUT-VI catalyzes alpha1,6-fucosylation of a dansylated asparagine-linked glycopeptide, which is derived from egg yolk
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Substrates: FucT3 and FucT5 possess alpha1,4FucT activity to fucosylate type 1 chains, but FucT3, as well as FucT6, account also for alpha3-fucosylation of type 2 chain in Colo205. FucT3 alone is responsible for synthesizing Lea and (sialyl) Lewis a, (sialyl)Galb1-(Fucalpha1-4)3GlcNAcbeta-(s)Lea in Colo205
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Substrates: alpha1,3-fucosyltransferase VII fucosylates sialylated acceptors and produces sialyl Lewis X antigens only
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Substrates: enzyme accepts fluorescein-isothiocyanate-labeled fucose and carboxyfluorescein-labeled fucose. Fluorescein-isothiocyanate-labeled NDP-beta-L-fucose is the best of these substrates
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Substrates: enzyme accepts fluorescein-isothiocyanate-labeled fucose and carboxyfluorescein-labeled fucose. Fluorescein-isothiocyanate-labeled NDP-beta-L-fucose is the best of these substrates
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Substrates: no activity with type 1 substrates
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Substrates: 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
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Substrates: 11 nonidentical amino acids, found within a hypervariable peptide segment positioned at the NH2 terminus determines whether or not an alpha(1,3)-fucosyltransferase can utilize type I acceptor substrates to form Lewis a and sialyl Lewis a moieties
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Substrates: the enzyme does not transfer efficiently to the isomeric oligosaccharide lacto-N-tetraose
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Substrates: the enzyme has acceptor specificity properties similar to that of the human myeloid enzyme FTIV
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Substrates: no activity with GalNAcbeta(1->4)GlcNAc-R
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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additional information
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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additional information
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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additional information
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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additional information
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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additional information
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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Substrates: evolution of vertebrate alpha-1,3/4-fucosyltransferases
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R115W/E116D
-
double mutation slightly increases H-type 1 activity
A128N
the mutant displays 3.4fold higher catalytic activity with D-lactose than the wild type enzyme
A128N/H129E
the mutant displays 6.5fold higher catalytic activity with D-lactose than the wild type enzyme
A128N/H129E/S46F
14.5fold improvement in specific activity
A128N/H129E/Y132I
9.6fold improvement in specific activity
A128N/H129E/Y132I/S46F
15.5fold improvement in specific activity
E338A/C(DELTA)74
6% decrease in alpha1,3-fucosyllactose yield
E338D
a strain expressing FucTa-E338D achieves 2.57 g/l alpha1,3-fucosyllactose, a 41.4% higher yield than that of the strain carrying the wild-type enzyme FucTa
F49K/Y131D/Y197N/E338D/R369A
-
best-performing mutant
G41E
150% increase in alpha1,3-fucosyllactose accumulation. The mutant exhibits an elevation in the production of byproducts
G41E/C(DELTA)74
52% decrease in alpha1,3-fucosyllactose yield
Y218K
the variant exhibits the highest alpha1,3-fucosyllactose yield, reaching 7.55 g/l in the shake flask growth experiment, which is 3.48-fold higher than that achieved by the wild-type enzyme. Subsequent fermentation optimization in a 5 l bioreactor resultsin a remarkable alpha1,3-fucosyllactose production of 36.98 g/l, highlighting the great prospects of the designed enzyme and the strains for industrial applications
Y218K/C(DELTA)74
67% decrease in alpha1,3-fucosyllactose yield
A349D
-
mutant enzyme shows higher activity with a range of acceptor substrates, higher affinity for Fucalpha(1,2)Galbeta(1,4)GlcNAc, 8fold higher overall catalytic efficiency than that of wild-type enzyme. The single amino acid site Asp336 of FucT III and Ala349 of FucT V constitutes the only difference in the sequence of FucT III and V over the final 210 COOH-terminal amino acid residues, impacts the acceptor substrate profiles of FucT III and FuvT V
C104S
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mutant enzyme is inactive, mutant enzyme produces a series of lower molecular weight bands when characterized by Wester blot and does not bind GDP
C351S
-
mutant enzyme is inactive
C354S
-
mutant enzyme is inactive
C64S
-
FucT V mutant is secreted exclusively as monomer
C94S
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mutant enzyme is inactive
N101Q/N153Q
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the mutations lead to an almost complete loss of enzymatic activity
N191Q/N153Q
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the mutant almost completely loses enzymatic activity
N17D
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the mutant is reactive toward lactose
K128D

26% increase in lacto-N-fucopentaose V biosynthesis
K128D
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26% increase in lacto-N-fucopentaose V biosynthesis
-
N101Q

-
the mutant shows about 30% of wild type activity
N101Q
-
the mutant still shows about 27% of wild type activity
N153Q

-
the mutant almost completely loses enzymatic activity
N153Q
-
the mutation leads to an almost complete loss of enzymatic activity
N62Q

-
the mutant shows about 60% of wild type activity
N62Q
-
the mutant still shows about 62% of wild type activity
N62Q/N101Q

-
the mutant almost completely loses enzymatic activity
N62Q/N101Q
-
the mutations lead to an almost complete loss of enzymatic activity
N62Q/N153Q

-
the mutant almost completely loses enzymatic activity
N62Q/N153Q
-
the mutations lead to an almost complete loss of enzymatic activity
additional information

-
with full length UA948FucT, 20% of total enzyme activities is localized in the soluble fraction. For UA948(1-428), this increases to 47%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. UA948(1-364), a mutant with the entire heptad repeat region removed, exhibits extremely low levels of enzyme activity. This indicates that the heptad repeat region is essential for enzyme activity. Construct alpha-(1,3/1,4)-fucosyltransferase(1-371) has little enzyme activity. alpha-(1,3/1,4)-fucosyltransferase(10-434) and alpha-(1,3/1,4)-fucosyltransferase(1-434) completely lose activity
additional information
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with full length 11639FucT, 28% of total enzyme activities is localized in the soluble fraction. For alpha-(1,3/1,4)-fucosyltransferase(1441), this increases to 45%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. Truncation mutant alpha-(1,3/1,4)-fucosyltransferase(10447) completely loses activity
additional information
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
additional information
J0U361
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
additional information
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
additional information
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
additional information
J0U361
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
additional information
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
additional information
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
additional information
J0U361
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
additional information
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
additional information
-
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
-
additional information
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wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
-
additional information
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the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
-
additional information
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with full length UA948FucT, 20% of total enzyme activities is localized in the soluble fraction. For UA948(1-428), this increases to 47%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. UA948(1-364), a mutant with the entire heptad repeat region removed, exhibits extremely low levels of enzyme activity. This indicates that the heptad repeat region is essential for enzyme activity. Construct alpha-(1,3/1,4)-fucosyltransferase(1-371) has little enzyme activity. alpha-(1,3/1,4)-fucosyltransferase(10-434) and alpha-(1,3/1,4)-fucosyltransferase(1-434) completely lose activity
-
additional information
-
with full length 11639FucT, 28% of total enzyme activities is localized in the soluble fraction. For alpha-(1,3/1,4)-fucosyltransferase(1441), this increases to 45%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. Truncation mutant alpha-(1,3/1,4)-fucosyltransferase(10447) completely loses activity
-
additional information
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with full length UA948FucT, 20% of total enzyme activities is localized in the soluble fraction. For UA948(1-428), this increases to 47%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. UA948(1-364), a mutant with the entire heptad repeat region removed, exhibits extremely low levels of enzyme activity. This indicates that the heptad repeat region is essential for enzyme activity. Construct alpha-(1,3/1,4)-fucosyltransferase(1-371) has little enzyme activity. alpha-(1,3/1,4)-fucosyltransferase(10-434) and alpha-(1,3/1,4)-fucosyltransferase(1-434) completely lose activity
-
additional information
-
with full length 11639FucT, 28% of total enzyme activities is localized in the soluble fraction. For alpha-(1,3/1,4)-fucosyltransferase(1441), this increases to 45%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. Truncation mutant alpha-(1,3/1,4)-fucosyltransferase(10447) completely loses activity
-
additional information
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catalytic domain of alpha-1,3-fucosyltransferase (amino acids 37-441) are expressed in Saccharomyces cerevisiae and Pichia pastoris as a fusion protein HSP150 delta-FucTe consisting of HSP150delta (1-321) and catalytic domain of FucTe (37-441) to promote proper folding and secretion
additional information
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Saccharomyces cerevisiae strain created co-expressing the catalytic domain of alpha-2,3-sialyltransferase and Fuc-Te in the cell wall, addition of N-acetyllactosamine, CMP-sialic acid and GDP-fucose results in the production of sLex
additional information
construction of mutants FUT9dcyt, FUT9d6, FUT9S/A, subcellular localization analysis of recombinant FUT9wt and mutants in HeLa cells
additional information
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construction of mutants FUT9dcyt, FUT9d6, FUT9S/A, subcellular localization analysis of recombinant FUT9wt and mutants in HeLa cells
additional information
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deletion of the -2,067 to -662 nt region enhances luciferase activity. The FUT VI promoter regions carrying deletions of conserved binding motifs are unaffected by overexpression of Oct-1 via transfection with pcDNA3.2/Oct--1
additional information
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primary adhesion of Th1 lymphocytes obtained from FucT-VII deficient mice is drastically reduced
additional information
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a marked reduction in formation of metastatic foci is observed in FucT7 deficient mice injected with murine colon carcinoma cells MC-38GFP
additional information
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O-linked oligosaccharides attached to GlyCAM-1 are analyzed in FucT-VII deficient mice, an 80% reduction in alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X and a significant increase in 6-sulfo N-acetyllactosamine are found in high-endothelial venules in secondary lymphoid organs of FucT-VII -/- mice, surprisingly, the amount of 6-sulfated galactose (Gal) is also increased in mutant mice, since 6-sulfo galactose can be synthesized by keratin sulfate sulfotransferase (KSST) it could be concluded that FucT-VII and KSST may compete for the same acceptor molecules
additional information
FT-IV deficient mice show a significant decrease in eosinophil recruitment to the skin
additional information
FT-IV deficient mice show a significant decrease in eosinophil recruitment to the skin
additional information
double knock-out mice deficient for both FT-IV and FT-VII show an essential absence of eosinophil recruitment to the dermis
additional information
double knock-out mice deficient for both FT-IV and FT-VII show an essential absence of eosinophil recruitment to the dermis
additional information
FT-VII deficient mice show a decrease in eosinophil recruitment to the skin
additional information
FT-VII deficient mice show a decrease in eosinophil recruitment to the skin
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Foster, C.S.; Gillies, D.R.B.; Glick, M.C.
Purification and characterization of GDP-L-Fuc-N-acetyl-beta-D-glucosaminide alpha1,3 fucosyltransferase from human neuroblastoma cells. Unusual substrate specificities of the tumor enzyme
J. Biol. Chem.
266
3526-3531
1991
Homo sapiens
brenda
Sarnesto, A.; Kohlin, T.; Hindsgaul, O.; Vogele, K.; Blaszczyk-Thurin, M.; Thurin, J.
Purification of the beta-N-acetylglucosaminide alpha 1,3-fucosyltransferase from human serum
J. Biol. Chem.
267
2745-2752
1992
Homo sapiens
brenda
Murray, B.W.; Takayama, S.; Schultz, J.; Wong, C.H.
Mechanism and specificity of human alpha-1,3-fucosyltransferase V
Biochemistry
35
11183-11195
1996
Homo sapiens
brenda
DeBose-Boyd, R.A.; Nyame, A.K.; Cummings, R.D.
Schistosoma mansoni: characterization of an alpha 1-3 fucosyltransferase in adult parasites
Exp. Parasitol.
82
1-10
1996
Schistosoma mansoni
brenda
DeBose-Boyd, R.A.; Nyame, A.K.; Cummings, R.D.
Molecular cloning and characterization of an alpha1,3 fucosyltransferase, CEFT-1, from Caenorhabditis elegans
Glycobiology
8
905-917
1998
Caenorhabditis elegans
brenda
Karaivanova, V.; Mookerjea, S.; Hunt, D.; Nagpurkar, A.
Characterization and purification of fucosyltransferases from the cytosol of rat colon
Int. J. Biochem. Cell Biol.
28
165-174
1996
Rattus norvegicus
brenda
Mulder, H.; Schachter, H.; Thomas, J.R.; Halkes, K.M.; Kamerling, J.P.; Vliegenthart, J.F.
Identification of a GDP-Fuc:Gal beta 1-3GalNAc-R (Fuc to Gal) alpha 1-2 fucosyltransferase and a GDP-Fuc:Gal beta 1-4GlcNAc (Fuc to GlcNAc) alpha 1-3 fucosyltransferase in connective tissue of the snail Lymnaea stagnalis
Glycoconjugate J.
13
107-113
1996
Lymnaea stagnalis
brenda
Legault, D.J.; Kelly, R.J.; Natsuka, Y.; Lowe, J.B.
Human alpha(1,3/1,4)-fucosyltransferases discriminate between different oligosaccharide acceptor substrates through a discrete peptide fragment
J. Biol. Chem.
270
20987-20996
1995
Homo sapiens
brenda
Holmes, E.H.; Yen, T.Y.; Thomas, S.; Joshi, R.; Nguyen, A.; Long, T.; Gallet, F.; Maftah, A.; Julien, R.; Macher, B.A.
Human alpha1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites
J. Biol. Chem.
275
24237-24245
2000
Homo sapiens
brenda
Dupuy, F.; Germot, A.; Marenda, M.; Oriol, R.; Blancher, A.; Julien, R.; Maftah, A.
alpha1,4-Fucosyltransferase activity: a significant function in the primate lineage has appeared twice independently
Mol. Biol. Evol.
19
815-824
2002
Homo sapiens, Macaca mulatta
brenda
Weston, B.W.; Nair, R.P.; Larsen, R.D.; Lowe, J.B.
Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities
J. Biol. Chem.
267
4152-4160
1992
Homo sapiens (Q11128)
brenda
Vo, L.; Lee, S.; Marcinko, M.C.; Holmes, E.H.; Macher, B.A.
Human alpha1,3/4-fucosyltransferases II. A single amino acid at the COOH terminus of FucT III and V alters their kinetic properties
J. Biol. Chem.
273
25250-25255
1998
Homo sapiens
brenda
Dupuy, F.; Petit, J.M.; Mollicone, R.; Oriol, R.; Julien, R.; Maftah, A.
A single amino acid in the hypervariable stem domain of vertebrate alpha1,3/1,4-fucosyltransferases determines the type 1/type 2 transfer. Characterization of acceptor substrate specificity of the Lewis enzyme by site-directed mutagenesis
J. Biol. Chem.
274
12257-12262
1999
Bos taurus
brenda
Costache, M.; Apoil, P.A.; Cailleau, A.; Elmgren, A.; Larson, G.; Henry, S.; Blancher, A.; Iordachescu, D.; Oriol, R.; Mollicone, R.
Evolution of fucosyltransferase genes in vertebrates
J. Biol. Chem.
272
29721-29728
1997
Pan troglodytes (P56434), Pan troglodytes (P56433)
brenda
Cameron, H.S.; Szczepaniak, D.; Weston, B.W.
Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms
J. Biol. Chem.
270
20112-20122
1995
Homo sapiens (Q11128), Homo sapiens (P51993)
brenda
Johnson, P.H.; Yates, A.D.; Watkins, W.M.
Human salivary fucosyltransferases: evidence for two distinct alpha-3-L-fucosyltransferase activities one or which is associated with the Lewis blood group Le gene
Biochem. Biophys. Res. Commun.
100
1611-1618
1981
Homo sapiens
brenda
Johnson, P.H.; Watkins, W.M.
Sialyl compounds as acceptor substrates for human alpha-3- and alpha-3/4-L-fucosyltransferases
Biochem. Soc. Trans.
13
1119-1120
1985
Homo sapiens
-
brenda
Johnson, P.H.; Watkins, W.M.
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Homo sapiens, Cricetulus griseus
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Homo sapiens
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Human myeloid alpha 3-fucosyltransferase is involved in the expression of the sialyl-Lewis(x) determinant, a ligand for E- and P-selectin
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Mus musculus (Q11131)
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Homo sapiens
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Rattus norvegicus (Q712G6)
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Mus musculus, Rattus norvegicus
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Synthesis of alpha(1,3) fucosyltransferases IV- and VII-dependent eosinophil selectin ligand and recruitment to the skin
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Homo sapiens, Mus musculus (Q11127), Mus musculus (Q11131)
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Rendic, D.; Klaudiny, J.; Stemmer, U.; Schmidt, J.; Paschinger, K.; Wilson, I.B.
Towards abolition of immunogenic structures in insect cells: characterization of a honey-bee (Apis mellifera) multi-gene family reveals both an allergy-related core alpha1,3-fucosyltransferase and the first insect Lewis-histo-blood-group-related antigen-synthesizing enzyme
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Apis mellifera (Q05GU1)
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Homo sapiens
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L-selectin facilitation of metastasis involves temporal induction of Fut7-dependent ligands at sites of tumor cell arrest
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Mus musculus
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Salo, H.; Sievi, E.; Suntio, T.; Mecklin, M.; Mattila, P.; Renkonen, R.; Makarow, M.
Co-expression of two mammalian glycosyltransferases in the yeast cell wall allows synthesis of sLex
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Homo sapiens
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Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing
Glycobiology
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2007
Mus musculus
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Efficient recruitment of lymphocytes in inflamed brain venules requires expression of cutaneous lymphocyte antigen and fucosyltransferase-VII
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Mus musculus
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Ma, B.; Audette, G.F.; Lin, S.; Palcic, M.M.; Hazes, B.; Taylor, D.E.
Purification, kinetic characterization, and mapping of the minimal catalytic domain and the key polar goups of Helicobacter pylori alpha-(1,3/1,4)-fucosyltransferases
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Helicobacter pylori, Helicobacter pylori NCTC11639, Helicobacter pylori UA948
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Homo sapiens
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Nguyen, K.; van Die, I.; Grundahl, K.M.; Kawar, Z.S.; Cummings, R.D.
Molecular cloning and characterization of the Caenorhabditis elegans alpha1,3-fucosyltransferase family
Glycobiology
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2007
Caenorhabditis elegans
brenda
Yang, X.; Zhang, Z.; Jia, S.; Liu, Y.; Wang, X.; Yan, Q.
Overexpression of fucosyltransferase IV in A431 cell line increases cell proliferation
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Homo sapiens (P22083)
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Moriguchi, K.; Takemoto, T.; Aoki, T.; Nakakita, S.; Natsuka, S.; Hase, S.
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Danio rerio
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Brito, C.; Escrevente, C.; Reis, C.A.; Lee, V.M.; Trojanowski, J.Q.; Costa, J.
Increased levels of fucosyltransferase IX and carbohydrate Lewis(x) adhesion determinant in human NT2N neurons
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Homo sapiens (Q5Q0U2), Homo sapiens
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Homo sapiens
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Brito, C.; Kandzia, S.; Graca, T.; Conradt, H.S.; Costa, J.
Human fucosyltransferase IX: specificity towards N-linked glycoproteins and relevance of the cytoplasmic domain in intra-Golgi localization
Biochimie
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2008
Homo sapiens (Q5Q0U2), Homo sapiens
brenda
Maeda, T.; Nishimura, S.
FRET-based direct and continuous monitoring of human fucosyltransferases activity: an efficient synthesis of versatile GDP-L-fucose derivatives from abundant D-galactose
Chemistry
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2008
Homo sapiens
brenda
Wang, H.; Wang, Q.Y.; Zhang, Y.; Shen, Z.H.; Chen, H.L.
Alpha1,3 Fucosyltransferase-VII modifies the susceptibility of apoptosis induced by ultraviolet and retinoic acid in human hepatocarcinoma cells
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Homo sapiens
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Lin, C.H.; Lin, C.W.; Khoo, K.H.
Proteomic identification of specific glycosyltransferases functionally implicated for the biosynthesis of a targeted glyco-epitope
Proteomics
8
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2008
Homo sapiens
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Gitlin, J.M.; Homeister, J.W.; Bulgrien, J.; Counselman, J.; Curtiss, L.K.; Lowe, J.B.; Boisvert, W.A.
Disruption of tissue-specific fucosyltransferase VII, an enzyme necessary for selectin ligand synthesis, suppresses atherosclerosis in mice
Am. J. Pathol.
174
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2009
Mus musculus
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Rouwendal, G.J.; Florack, D.E.; Hesselink, T.; Cordewener, J.H.; Helsper, J.P.; Bosch, D.
Synthesis of Lewis X epitopes on plant N-glycans
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Tetraodon nigroviridis (Q6EV15)
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Stacke, C.; Ziegelmueller, P.; Hahn, U.
Comparison of expression systems for human fucosyltransferase IX
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2010
Homo sapiens
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Norden, R.; Nystroem, K.; Olofsson, S.
Activation of host antiviral RNA-sensing factors necessary for herpes simplex virus type 1-activated transcription of host cell fucosyltransferase genes FUT3, FUT5, and FUT6 and subsequent expression of sLe(x) in virus-infected cells
Glycobiology
19
776-788
2009
Homo sapiens
brenda
Carvalho, A.; Harduin-Lepers, A.; Magalhaes, A.; Machado, E.; Mendes, N.; Costa, L.; Matthiesen, R.; Almeida, R.; Costa, J.; Reis, C.
Differential expression of alpha-2,3-sialyltransferases and alpha-1,3/4-fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells
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42
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2010
Homo sapiens (P51993), Homo sapiens (P22083), Homo sapiens (Q9Y231)
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Wang, Q.Y.; Zhang, Y.; Shen, Z.H.; Chen, H.L.
alpha1,3 fucosyltransferase-VII up-regulates the mRNA of alpha5 integrin and its biological function
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Homo sapiens
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Chemoenzymatic synthesis of GDP-L-fucose and the Lewis X glycan derivatives
Proc. Natl. Acad. Sci. USA
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2009
Helicobacter pylori (O25366)
brenda
Ponnampalam, A.P.; Rogers, P.A.
Expression and regulation of fucosyltransferase 4 in human endometrium
Reproduction
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2008
Homo sapiens
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Guo, Q.; Guo, B.; Wang, Y.; Wu, J.; Jiang, W.; Zhao, S.; Qiao, S.; Wu, Y.
Functional analysis of alpha1,3/4-fucosyltransferase VI in human hepatocellular carcinoma cells
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Homo sapiens
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Laporte, B.; Petit, D.; Rocha, D.; Boussaha, M.; Grohs, C.; Maftah, A.; Petit, J.
Characterization of bovine FUT7 furthers understanding of FUT7 evolution in mammals
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Bos taurus (A1XCQ0), Bos taurus
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Seelhorst, K.; Stacke, C.; Ziegelmueller, P.; Hahn, U.
N-Glycosylations of human alpha1,3-fucosyltransferase IX are required for full enzyme activity
Glycobiology
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2013
Homo sapiens
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Li, W.; Zhang, W.; Luo, J.; Cao, A.; Zhang, Y.; Huang, D.; Sheng, W.; Cai, S.; Li, J.
Alpha1,3 Fucosyltransferase VII plays a role in colorectal carcinoma metastases by promoting the carbohydration of glycoprotein CD24
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Homo sapiens
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Choi, Y.H.; Kim, J.H.; Park, B.S.; Kim, B.G.
Solubilization and iterative saturation mutagenesis of alpha1,3-fucosyltransferase from Helicobacter pylori to enhance its catalytic efficiency
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2016
Helicobacter pylori (O25142)
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Lee, J.; Pandey, R.; Kim, D.; Sohng, J.
Cloning and functional characterization of an alpha-1,3-fucosyltransferase from Bacteroides fragilis
Biotechnol. Bioprocess Eng.
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Bacteroides fragilis, Bacteroides fragilis NCTC 9343
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Yang, X.; Liu, S.; Yan, Q.
Role of fucosyltransferase IV in epithelial-mesenchymal transition in breast cancer cells
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Homo sapiens (P22083)
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Mickum, M.L.; Rojsajjakul, T.; Yu, Y.; Cummings, R.D.
Schistosoma mansoni alpha1,3-fucosyltransferase-F generates the Lewis X antigen
Glycobiology
26
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2016
Schistosoma mansoni
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Ebel, M.E.; Kansas, G.S.
Defining the functional boundaries of the murine alpha1,3-fucosyltransferase Fut7 reveals a remarkably compact locus
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Mus musculus
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Helicobacter pylori (O30511)
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Biochemical characterization of Helicobacter pylori alpha1-3-fucosyltransferase and its application in the synthesis of fucosylated human milk oligosaccharides
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Helicobacter pylori (O30511)
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Seelhorst, K.; Pahnke, K.; Meier, C.; Hahn, U.
Tagging glycoproteins with fluorescently labeled GDP-fucoses by Using alpha1,3-fucosyltransferases
ChemBioChem
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2015
Helicobacter pylori (O30511), Homo sapiens (Q11130), Homo sapiens (Q9Y231)
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Mercx, S.; Smargiasso, N.; Chaumont, F.; De Pauw, E.; Boutry, M.; Navarre, C.
Inactivation of the beta(1,2)-xylosyltransferase and the alpha(1,3)-fucosyltransferase genes in Nicotiana tabacum BY-2 cells by a Multiplex CRISPR/Cas9 strategy results in glycoproteins without plant-specific glycans
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Nicotiana tabacum
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Li, D.; Sun, H.; Bai, G.; Wang, W.; Liu, M.; Bao, Z.; Li, J.; Liu, H.
alpha-1,3-Fucosyltransferase-VII siRNA inhibits the expression of SLex and hepatocarcinoma cell proliferation
Int. J. Mol. Med.
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2018
Homo sapiens
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Zhang, J.; Ju, N.; Yang, X; Chen, L.; Yu, C.
The alpha1,3-fucosyltransferase FUT7 regulates IL-1beta-induced monocyte-endothelial adhesion via fucosylation of endomucin
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Homo sapiens
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Yu, J.; Shin, J.; Park, M.; Seydametova, E.; Jung, S.M.; Seo, J.H.; Kweon, D.H.
Engineering of alpha-1,3-fucosyltransferases for production of 3-fucosyllactose in Escherichia coli
Metab. Eng.
48
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2018
Helicobacter pylori (O25366), Helicobacter pylori (J0U361), Helicobacter pylori (O25142), Helicobacter pylori ATCC 43504 (J0U361), Helicobacter pylori ATCC 700392 (O25142), Helicobacter pylori ATCC 700392 (O25366)
brenda
Pedersen, C.T.; Loke, I.; Lorentzen, A.; Wolf, S.; Kamble, M.; Kristensen, S.K.; Munch, D.; Radutoiu, S.; Spillner, E.; Roepstorff, P.; Thaysen-Andersen, M.; Stougaard, J.; Dam, S.
N-glycan maturation mutants in Lotus japonicus for basic and applied glycoprotein research
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Lotus japonicus
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Wang, N.; Zhu, Y.; Wang, L.; Huang, Z.; Li, Z.; Xu, W.; Mu, W.
Highly-efficient in vivo production of lacto-N-fucopentaose V by a regio-specific alpha1,3/4-fucosyltransferase from Bacteroides fragilis NCTC 9343
Int. J. Biol. Macromol.
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Bacteroides fragilis (Q5L9S6), Bacteroides fragilis NCTC 9343 (Q5L9S6)
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Shan, X.; Dong, W.; Zhang, L.; Cai, X.; Zhao, Y.; Chen, Q.; Yan, Q.; Liu, J.
Role of fucosyltransferase IV in the migration and invasion of human melanoma cells
IUBMB Life
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942-956
2020
Homo sapiens (P22083)
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Xie, Y.; Wu, X.; Fu, C.; Duan, H.; Shi, J.; Blamey, J.M.; Sun, J.
Rational design of an alpha-1,3-fucosyltransferase for the biosynthesis of 3-fucosyllactose in Bacillus subtilis ATCC 6051a via de novo GDP-L-fucose pathway
J. Agric. Food Chem.
72
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Helicobacter pylori (Q9L8S4)
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Zhu, Y.; Chen, R.; Wang, H.; Chen, Y.; Huang, Z.; Du, Z.; Meng, J.; Zhou, J.; Mu, W.
De novo biosynthesis of difucosyllactose by artificial pathway construction and alpha1,3/4-fucosyltransferase rational design in Escherichia coli
J. Agric. Food Chem.
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Helicobacter pylori
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Sugita, T.; Sampei, S.; Koketsu, K.
Efficient production of lacto-N-fucopentaose III in engineered Escherichia coli using alpha1,3-fucosyltransferase from Parabacteroides goldsteinii
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Parabacteroides goldsteinii
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Magdaleno, J.S.L.; Grewal, R.K.; Medina-Franco, J.L.; Oliva, R.; Shaikh, A.R.; Cavallo, L.; Chawla, M.
Toward alpha-1,3/4 fucosyltransferases targeted drug discovery In silico uncovering of promising natural inhibitors of fucosyltransferase 6
J. Cell. Biochem.
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2023
Homo sapiens (P51993)
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Kadirvelraj, R.; Boruah, B.M.; Wang, S.; Chapla, D.; Huang, C.; Ramiah, A.; Hudson, K.L.; Prudden, A.R.; Boons, G.J.; Withers, S.G.; Wood, Z.A.; Moremen, K.W.
Structural basis for Lewis antigen synthesis by the alpha1,3-fucosyltransferase FUT9
Nat. Chem. Biol.
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1022-1030
2023
Homo sapiens (Q9Y231)
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Chaubey, S.; Nader, Y.M.; Shah, D.; Kumova, O.K.; Prahaladan, V.; Carey, A.J.; Andersson, S.; Bhandari, V.
alpha1,3-Fucosyltransferase-IX, an enzyme of pulmonary endogenous lung stem cell marker SSEA-1, alleviates experimental bronchopulmonary dysplasia
Pediatr. Res.
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2021
Mus musculus (O88819), Homo sapiens (Q9Y231)
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Jung, J.W.; Shin, J.H.; Lee, W.K.; Begum, H.; Min, C.H.; Jang, M.H.; Oh, H.B.; Yang, M.S.; Kim, S.R.
Inactivation of the beta (1, 2)-xylosyltransferase and the alpha (1, 3)-fucosyltransferase gene in rice (Oryza sativa) by multiplex CRISPR/Cas9 strategy
Plant Cell Rep.
40
1025-1035
2021
Oryza sativa
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