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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
-
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
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
FucT-VII and FucT-IV
-
-
?
GDP-beta-fucose + alpha2,3-sialyl N-acetyllactosaminyl-R
GDP + alpha1,3-fucosyl-alpha2,3-sialyl-N-acetyllactosaminyl-R
-
FucT-VII and FucT-IV
-
-
?
GDP-beta-fucose + lacto-N-neotetraose
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc
-
-
-
?
GDP-beta-fucose + lactose
GDP + alpha1,3-fucosyllactose
N-acetyllactosamine is preferred over lactose
-
-
?
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
?
-
8% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + alpha(2,3) bisialylated biantennary glycan
?
-
-
-
-
?
GDP-beta-L-fucose + asialo-erythropoietin
?
wild-type FUT9 efficiently fucosylates di-, tri- and tetraantennary N-glycans from asialoEPO
-
-
?
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
-
-
-
-
?
GDP-beta-L-fucose + D-lactose
GDP + 3 L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-Glc
-
the enzyme has very low relative substrate specificity toward D-lactose
-
-
?
GDP-beta-L-fucose + fetuin
?
-
-
-
-
?
GDP-beta-L-fucose + fetuin-biotin
?
-
-
-
-
?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
GDP-beta-L-fucose + Galbeta1,4GlcNAc
?
-
-
-
-
?
GDP-beta-L-fucose + Galbeta1-4GlcNAcalpha-4-nitrophenol
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcalpha-4-nitrophenol
-
preferred substrate of CEFT-4 and CEFT-3
-
-
?
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 + N-acetyl-D-lactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
GDP-beta-L-fucose + N-acetyllactosamine
GDP + ?
-
-
-
-
?
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
?
-
i.e. 6-sulfo-3'SLN, best substrate
-
-
?
GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-GlcNAc beta-(1,3)-Galbeta-(1,4)-Glcbeta-O-C3H6-biotin
?
-
i.e. 3'SLNL
-
-
?
GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-GlcNAc beta-O-BSA-biotin
?
-
i.e. 3'SLN-BSA
-
-
?
GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-GlcNAc beta-O-C3H6-biotin
?
-
i.e. 3'SLN
-
-
?
GDP-beta-L-fucose + Neu5Acalpha-(2,3)-Galbeta-(1,4)-GlcNAcbeta-R
GDP + Neu5Acalpha-(2,3)-Galbeta-(1,4)-[Fucalpha-(1,3)]-GlcNAcbeta-R
-
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
i.e. antigen sLex
-
?
GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3]-GlcNAc-R
-
sialyl-Lewisx terminal structure
-
-
?
GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)[SO3H-6]-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3][SO3H-6]-GlcNAc-R
-
sialyl-Lewisx terminal structure
-
-
?
GDP-beta-L-fucose + NeuAcalpha(2,3)Galbeta(1,4)Glc
?
-
-
-
-
?
GDP-beta-L-fucose + NeuAcalpha2,3Galbeta1,4GlcNAc
?
-
32% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + NeuNAcalpha(2->3)Galbeta(1->4)GlcNAc
GDP + NeuNAcalpha(2->3)Galbeta(1->4)[L-Fucalpha(1->3)]GlcNAc
best substrate
-
-
?
GDP-beta-L-fucose + octyl Galbeta(1->4)GlcNAc
GDP + octyl Galbeta(1->4)[L-Fucalpha(1->3)]GlcNAc
-
-
-
?
GDP-beta-L-fucose + unsialylated biantennary glycan
?
-
-
-
-
?
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
-
-
-
?
GDP-fucose + (-3GalNAcbeta1-4GlcNAcbeta1-)n
GDP + (-3GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-)n
-
-
N-glycans containing poly-LDN structures are efficiently fucosylated by human FucT9 producing poly-LDNF structures, max. 4-6 repeating LDNF units
-
?
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
-
oligosaccharides are determined by a combination of exoglycosidase digestions and two-dimensional HPLC sugar mapping, most of these oligosaccharides are free form
-
-
?
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
-
-
-
-
?
GDP-fucose + asialo human erythropoietin
GDP + fucosylated asialo human erythropoietin
-
-
-
-
?
GDP-fucose + bovine asialofetuin
GDP + fucosylated bovine asialofetuin
-
-
-
-
?
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAc
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc
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
-
-
-
-
?
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAcbeta1-R
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-R
-
Lewis Y antigen, increased expression in cancer cells
-
?
GDP-fucose + Galbeta(1,3)GlcNAcOMe
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcOMe
-
-
-
-
?
GDP-fucose + Galbeta1-4Glc
GDP + Galbeta1-4 (Fucalpha1-3)Glc
-
-
-
?
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
-
-
-
-
?
GDP-fucose + Galbeta1-4GlcNAc
GDP + Galbeta1-4 (Fucalpha1-3)GlcNAc
-
-
-
?
GDP-fucose + Galbeta1-4GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
-
sFUT9 efficiently fucosylates type II acceptors but not the corresponding sialylated acceptors, and only very poorly the type I (Galbeta3GlcNAc-R) related acceptors
-
-
?
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
-
-
-
?
GDP-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-PA
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc-PA
Lacto-N-neo-tetraose is a Lewis-type FucT substrate
-
-
?
GDP-fucose + GalNAcbeta1-4GlcNAcbeta-R
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-R
-
-
-
-
?
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
-
-
-
?
GDP-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + GalNAcbeta1-4[Fucalpha1-3]GlcNAcbeta1-3Galbeta1-4Glc
-
incubation with extracts from transfected COS7 cells
product obtained at a level of about 50% of that obtained with the acceptor GalNAcbeta1-4GlcNAcbeta1-R
?
GDP-fucose + GalNAcbeta1-4GlcNAcbeta1-R
GDP + GalNAcbeta1-4[Fucalpha1-3]GlcNAcbeta1-R
-
-
-
?
GDP-fucose + human erythropoietin
GDP + fucosylated human erythropoietin
-
-
-
-
?
GDP-fucose + LacNAc
GDP + ?
-
-
-
?
GDP-fucose + LacNAcbeta-O-(CH2)5CO2CH3
GDP + ?
-
-
-
?
GDP-fucose + lacto-N-neotetraose
GDP + ?
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
GDP-L-fucose + 2'-fucosyllactose
GDP + ?
42% of the activity with Galbeta(1,4)GlcNAc
-
-
?
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
-
-
-
?
GDP-L-fucose + 3'-sialyl N-acetyl lactosamine
GDP + ?
-
-
-
-
?
GDP-L-fucose + alpha(2,3)-sialyllactosamine
GDP + ?
-
115% of the activity with Galbeta(1,4)GlcNAc
-
-
?
GDP-L-fucose + alpha(2,3)sialyllactosamine
GDP + ?
-
-
-
?
GDP-L-fucose + alpha1 acid glycoprotein
GDP + ?
-
with the major terminal structure on N-linked chains: NeuAc(2,3/6)Galbeta(1,4)GlcNAcbeta-R
-
-
?
GDP-L-fucose + asialo-alpha1-acid glycoprotein
GDP + ?
-
with the major terminal structure on N-linked chains: Galbeta(1,4)GlcNAcbeta-R
-
-
?
GDP-L-fucose + asialo-fetuin
GDP + ?
-
with the major terminal structure on N-linked chains: Galbeta(1,4)GlcNAcbeta-R
-
-
?
GDP-L-fucose + asialotransferrin
GDP + ?
-
-
-
-
?
GDP-L-fucose + desialylated alpha1-acid glycoprotein
GDP + ?
-
-
-
-
?
GDP-L-fucose + fetuin
GDP + ?
GDP-L-fucose + fetuin
GDP + alpha1,3-L-fucosyl-fetuin
-
FucT-VI
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
GDP-L-fucose + Galalpha(1,3)Galbeta(1,4)GlcNAc-R
GDP + ?
GDP-L-fucose + Galbeta(1,3)GlcNAc
GDP + ?
i.e. lacto-N-biose I, 10% of the activity with Galbeta(1,4)GlcNAc
-
-
?
GDP-L-fucose + Galbeta(1,4)-Glc
GDP + Galbeta(1,4)(Fucalpha(1,3))Glc
-
3% of the activity with Galbeta(1,4)GlcNAc
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
GDP-L-fucose + lacto-N-biose I
GDP + ?
-
-
-
?
GDP-L-fucose + lacto-N-fucopentaose I
GDP + ?
-
-
-
-
?
GDP-L-fucose + lacto-N-fucopentaose II
GDP + ?
-
-
-
-
?
GDP-L-fucose + lacto-N-neotetraose
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
-
-
-
?
GDP-L-fucose + lacto-N-tetraose
GDP + ?
-
-
-
-
?
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
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
-
-
-
-
?
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
-
-
-
-
?
GDP-L-fucose + sialyl-alpha-2,3-N-acetyllactosamine
GDP + NeuNAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAc
-
-
-
?
additional information
?
-
GDP-alpha-L-fucose + asialofetuin
GDP + ?
-
-
-
?
GDP-alpha-L-fucose + asialofetuin
GDP + ?
-
-
-
?
GDP-alpha-L-fucose + fetuin
GDP + ?
-
-
-
?
GDP-alpha-L-fucose + fetuin
GDP + ?
-
-
-
?
GDP-alpha-L-fucose + glycoprotein gp130
GDP + ?
-
-
-
?
GDP-alpha-L-fucose + glycoprotein gp130
GDP + ?
-
-
-
?
GDP-beta-fucose + N-acetyllactosamine
GDP + alpha1,3-fucosyl-N-acetyllactosamine
N-acetyllactosamine is preferred over lactose. At a low GDP-fucose to acceptor ratio, the enzyme selectively fucosylates N-acetyllactosamine
-
-
?
GDP-beta-fucose + N-acetyllactosamine
GDP + alpha1,3-fucosyl-N-acetyllactosamine
-
FucT-VI
-
-
?
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc
?
-
135% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc
?
-
72% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
-
115% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
-
99% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
-
activity of CEFT-3 aqnd CEFT-4
-
-
?
GDP-beta-L-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
-
substrate of CEFT-3
-
-
?
GDP-beta-L-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
-
activity of CEFT-2
-
-
?
GDP-beta-L-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
activity of CEFT-2
-
-
?
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-acetyl-D-lactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
-
-
-
-
?
GDP-beta-L-fucose + N-acetyllactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
-
-
-
-
?
GDP-beta-L-fucose + N-acetyllactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
-
-
-
-
?
GDP-beta-L-fucose + N-acetyllactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
-
-
-
-
?
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAc
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc
-
-
-
?
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAc
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc
-
-
-
?
GDP-fucose + Galbeta1-4GlcNAc-R
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-R
-
-
Lewis x determinant
?
GDP-fucose + Galbeta1-4GlcNAc-R
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-R
-
-
Lewis x determinant
?
GDP-fucose + lacto-N-neotetraose
GDP + lacto-N-fucopentaose III
-
-
-
?
GDP-fucose + lacto-N-neotetraose
GDP + lacto-N-fucopentaose III
-
-
-
?
GDP-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc
GDP + NeuAcalpha2-3Galbeta1-4(Fucalpha1-3)GlcNAc
-
-
sialyl Lewis x
?
GDP-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc
GDP + NeuAcalpha2-3Galbeta1-4(Fucalpha1-3)GlcNAc
-
-
-
?
GDP-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc
GDP + NeuAcalpha2-3Galbeta1-4(Fucalpha1-3)GlcNAc
-
rate of reaction below 5% of the rate obtained toward nonsialylated acceptor
sialyl Lewis x
?
GDP-L-fucose + fetuin
GDP + ?
-
with the major terminal structure on N-linked chains: NeuAcalpha(2,3/6)Galbeta(1,4)GlcNAcbeta-R
-
-
?
GDP-L-fucose + fetuin
GDP + ?
-
-
-
-
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,3)GlcNAc-R
GDP + ?
-
-
-
-
?
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)Glc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))Glc
-
-
-
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)Glc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))Glc
-
i.e. 2'-fucosyllactose, 17% of the activity with Galbeta(1,4)GlcNAc
-
-
?
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)GlcNAc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
162% of the activity with Galbeta(1,4)GlcNAc
-
-
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
mutant enzyme A349D shows 8fold higher activity than the wild-type enzyme
-
-
?
GDP-L-fucose + Galalpha(1,3)Galbeta(1,4)GlcNAc-R
GDP + ?
-
-
-
-
?
GDP-L-fucose + Galalpha(1,3)Galbeta(1,4)GlcNAc-R
GDP + ?
-
-
-
-
?
GDP-L-fucose + Galbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
-
-
?
GDP-L-fucose + Galbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
i.e. N-acetyllactosamine
-
-
?
GDP-L-fucose + Galbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
i.e. N-acetyllactosamine
-
-
?
GDP-L-fucose + Galbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
i.e. N-acetyllactosamine
-
?
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-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)GlcNAc-R
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-R
-
-
-
-
?
GDP-L-fucose + lactose
GDP + ?
-
-
-
-
?
GDP-L-fucose + lactose
GDP + ?
-
weak activity
-
-
?
GDP-L-fucose + lactose
GDP + ?
11% of the activity with Galbeta(1,4)GlcNAc
-
-
?
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
-
-
-
?
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
-
-
-
?
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)GlcNAc
GDP + NeuAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
-
147% of the activity with Galbeta(1,4)GlcNAc
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
native enzyme utilizes only type 2 acceptors. Double mutation R115W/E116D slightly increases H-type 1 activity
-
-
?
additional information
?
-
no activity with Galbeta(1-3)GlcNAc-octyl, NeuAcalpha(2,3)Galbeta(1,3)GlcNAc and Fucalpha(1,2) Galalpha(1,4)GlcNAc
-
-
?
additional information
?
-
-
no activity with Galbeta(1-3)GlcNAc-octyl, NeuAcalpha(2,3)Galbeta(1,3)GlcNAc and Fucalpha(1,2) Galalpha(1,4)GlcNAc
-
-
?
additional information
?
-
-
the enzyme has acceptor specificity properties similar to that of the human myeloid enzyme FTIV
-
-
?
additional information
?
-
-
the recombinant enzyme has a clear preference for nonsialylated type-2 acceptors over either neutral type-1 acceptors or sialylated type-2 acceptors
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
-
the enzyme shows alpha1,3- and alpha1,4-fucosyltransferase activity
-
-
?
additional information
?
-
enzyme accepts fluorescein-isothiocyanate-labeled fucose and carboxyfluorescein-labeled fucose. Fluorescein-isothiocyanate-labeled NDP-beta-L-fucose is the best of these substrates
-
-
-
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
lactose and its fucose-substituted derivative are very poor acceptors for the enzyme
-
-
?
additional information
?
-
-
acceptor: type 2 H-oligosaccharide 8-methoxycarbonyloctyl glycoside
-
-
?
additional information
?
-
-
weak activity with type 1 substrates
-
-
?
additional information
?
-
-
acceptor specificity with glycoprotein and glycolipid acceptors
-
-
?
additional information
?
-
-
fetuin and asialofetuin bearing N-linked carbohydrate chains containing the type II lactosamine core (Galbeta(1,4)GlcNAc)
-
-
?
additional information
?
-
-
predominantly activity with sialylated or nonsialylated type-2 chain acceptors, only a low alpha(1,4)-fucosyltransferase activity with type-1 chain acceptors
-
-
?
additional information
?
-
-
no activity with Galbeta(1,3)GlcNAc, NeuAcalpha2,6Galbeta(1,4)GlcNAc, NeuAcalpha2,8NeuAc and NeuAcalpha2,6Galbeta(1,4)Glc
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme is involved in the expression of the sialyl-LewisX determinant, a ligand for E- and P-selectin
-
-
?
additional information
?
-
-
the hepatocellular enzyme is involved in the synthesis of sialosyl LeX determinants on cirrhotic alpha1AGP
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
assay development utilizing anion exchange chromatography
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
-
recombinant alpha1,3FucT-VII acts as a potential antiapoptotic factor in H7721 cells after induction of apoptosis by UV irradiation, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
FUT-VI catalyzes alpha1,6-fucosylation of a dansylated asparagine-linked glycopeptide, which is derived from egg yolk
-
-
?
additional information
?
-
-
alpha1,3-fucosyltransferase VII fucosylates sialylated acceptors and produces sialyl Lewis X antigens only
-
-
?
additional information
?
-
enzyme accepts fluorescein-isothiocyanate-labeled fucose and carboxyfluorescein-labeled fucose. Fluorescein-isothiocyanate-labeled NDP-beta-L-fucose is the best of these substrates
-
-
-
additional information
?
-
enzyme accepts fluorescein-isothiocyanate-labeled fucose and carboxyfluorescein-labeled fucose. Fluorescein-isothiocyanate-labeled NDP-beta-L-fucose is the best of these substrates
-
-
-
additional information
?
-
-
no activity with type 1 substrates
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme does not transfer efficiently to the isomeric oligosaccharide lacto-N-tetraose
-
-
?
additional information
?
-
-
the enzyme has acceptor specificity properties similar to that of the human myeloid enzyme FTIV
-
-
?
additional information
?
-
-
no activity with GalNAcbeta(1->4)GlcNAc-R
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
additional information
?
-
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
?
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0.65
3'-sialyl N-acetyl lactosamine
-
pH 7.2, 37°C
0.00094
6-deoxy-6-N-(2-naphthalene-2-yl-acetamide)-beta-L-galactopyranos-1-yl-guanosine 5'-diphosphate disodium salt
-
pH 7.5, 25°C
1.4
6-deoxy-alpha-L-galactopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranose
-
pH 7.6, 15 mM MnCl2, 0.095 mM GDP-fucose
0.38
alpha(2,3) bisialylated biantennary glycan
-
pH 7.2, 37°C
-
7.8
alpha2,3-sialyl-N-acetyllactosamine
-
pH 6.5, 30°C, recombinant FucT-VII
6.7 - 20
Fucalpha(1,2)Galbeta(1,4)Glc
0.7 - 3.9
Fucalpha(1,2)Galbeta(1,4)GlcNAc
1
Fucalpha1-2Galbeta1-4Glc
-
-
17
Gal-beta-(1->3)-[Fuc-alpha-(1->4)-])GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
pH 7.6, 15 mM MnCl2, 0.095 mM GDP-fucose
0.35
Galbeta(1,3)GlcNAcOMe
-
-
1.4 - 23
Galbeta(1,4)GlcNAc
1.5
Galbeta(1,4)GlcNAcbeta(1,3)Galbeta(1,4)Glc
-
pH 7.3, 37°C
0.37 - 1.7
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
0.021 - 6.448
GDP-beta-fucose
0.00012 - 1.12
GDP-beta-L-fucose
0.0055 - 0.062
GDP-L-fucose
0.17
LacNAcbeta-O-(CH2)5CO2CH3
-
-
0.3 - 0.76
lacto-N-neotetraose
5
lacto-N-tetraose
-
pH 7.6, 15 mM MnCl2, 0.095 mM GDP-fucose
0.075
methyl beta-D-2-O-methylgalactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
-
-
0.12
methyl beta-D-2-O-methylgalactosyl-(1-4)-6-O-methyl-N-acetyl-beta-D-glucosamine
-
-
0.39
methyl beta-D-2-O-methylgalactosyl-(1-4)-N-acetyl-beta-D-glucosamine
-
-
0.19
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-acetylamino-beta-D-glucopyranose
-
-
0.4
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-amino-beta-D-glucopyranose
-
-
0.14
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
-
-
0.115
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-methylsulfonylamino-beta-D-glucopyranose
-
-
1.54
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl amide
-
-
0.29
methyl beta-D-galactosyl-(1-4)-6-O-methyl-N-acetyl-beta-D-glucosamine
-
-
0.25
methyl beta-D-galactosyl-(1-4)-6-O-methylsulfonyl-N-acetyl-beta-D-glucosamine
-
-
0.45
methyl beta-D-galactosyl-(1->4)-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl ester
-
-
2.6
N-acetyl lactosamine
-
pH 7.2, 37°C
0.53
N-acetyl-beta-lactosamine
-
-
0.0026 - 0.61
N-acetyllactosamine
0.05
Neu5Acalpha(2,3)-Galbeta(1,4)-6-O-sulfo-GlcNAc beta-O-C3H6-biotin
-
pH 7.4, 22°C
3.9
NeuAcalpha(2,3)Galbeta(1,4)Glc
-
-
0.2 - 0.9
NeuAcalpha(2,3)Galbeta(1,4)GlcNAc
0.96
NeuAcalpha2-3Galbeta1-4GlcNAc
-
-
1.7
sialyl-alpha-2,3-N-acetyllactosamine
-
fusion protein Hsp150delta-FucTe
0.74
unsialylated biantennary glycan
-
pH 7.2, 37°C
-
additional information
additional information
-
-
-
72
D-lactose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
81
D-lactose
-
mutant enzyme A128N/H129E/S46F, at pH 7.6 and 37°C
97
D-lactose
-
mutant enzyme A128N/H129E/Y132I, at pH 7.6 and 37°C
123
D-lactose
-
mutant enzyme A128N/H129E, at pH 7.6 and 37°C
232
D-lactose
-
mutant enzyme A128N, at pH 7.6 and 37°C
543
D-lactose
-
wild type enzyme, at pH 7.6 and 37°C
6.7
Fucalpha(1,2)Galbeta(1,4)Glc
-
-
20
Fucalpha(1,2)Galbeta(1,4)Glc
-
pH 7.6, 15 mM MnCl2, 0.095 mM GDP-fucose
0.7
Fucalpha(1,2)Galbeta(1,4)GlcNAc
-
-
1.1
Fucalpha(1,2)Galbeta(1,4)GlcNAc
-
fucosyltransferase V mutant enzyme A349D
1.3
Fucalpha(1,2)Galbeta(1,4)GlcNAc
-
-
3.9
Fucalpha(1,2)Galbeta(1,4)GlcNAc
-
fucosyltransferase V
1.4
Galbeta(1,4)GlcNAc
-
-
2.9
Galbeta(1,4)GlcNAc
-
pH 7.3, 37°C
23
Galbeta(1,4)GlcNAc
-
pH 7.0, 37°C
0.37
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
full-length enzyme
0.39
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1441)
1.5
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
full-length enzyme
1.7
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1428)
0.021
GDP-beta-fucose
-
pH 6.5, 30°C, recombinant FucT-VII and commercial FucT-VI
5.3392
GDP-beta-fucose
cosubstrate lactose, pH 7.5, 37°C
6.448
GDP-beta-fucose
cosubstrate N-acetyllactosamine, pH 7.5, 37°C
0.00012
GDP-beta-L-fucose
-
pH 7.4, 22°C
0.0026
GDP-beta-L-fucose
-
wild type enzyme, in citrate/phosphate buffer, pH 4.5, at 37°C
0.0026
GDP-beta-L-fucose
-
recombinant wild type enzyme, at pH 4.5 and 37°C
0.0047
GDP-beta-L-fucose
-
mutant enzyme N101Q, in citrate/phosphate buffer, pH 4.5, at 37°C
0.0047
GDP-beta-L-fucose
-
mutant enzyme N101Q, at pH 4.5 and 37°C
0.0061
GDP-beta-L-fucose
-
mutant enzyme N62Q, at pH 4.5 and 37°C
0.0066
GDP-beta-L-fucose
-
mutant enzyme N62Q, in citrate/phosphate buffer, pH 4.5, at 37°C
0.0156
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1441)
0.0176
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1428)
0.0447
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, full-length enzyme
0.056
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, full-length enzyme
0.24
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I, at pH 7.6 and 37°C
0.28
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/S46F, at pH 7.6 and 37°C
0.3
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
0.33
GDP-beta-L-fucose
-
wild type enzyme, at pH 7.6 and 37°C
0.37
GDP-beta-L-fucose
-
mutant enzyme A128N, at pH 7.6 and 37°C
0.37
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E, at pH 7.6 and 37°C
1.12
GDP-beta-L-fucose
-
at pH 7.5 and 37°C
0.0016
GDP-fucose
-
pH 6.5, 37°C
0.0065
GDP-fucose
-
pH 7.2, 37°C
0.025
GDP-fucose
-
LacNAcbeta-O-(CH2)5CO2CH3 as substrate
0.06
GDP-fucose
-
LacNAc as substrate
0.0055
GDP-L-fucose
-
pH 7.5, 25°C
0.0188
GDP-L-fucose
-
fucosyltransferase V
0.0233
GDP-L-fucose
-
fucosyltransferase V mutant enzyme A349D
0.062
GDP-L-fucose
-
pH 7.6, 15 mM MnCl2
0.3
lacto-N-neotetraose
-
-
0.76
lacto-N-neotetraose
-
-
3.729
lactose
pH 7.5, 37°C
83
lactose
-
pH 7.6, 15 mM MnCl2, 0.095 mM GDP-fucose
0.0026
N-acetyllactosamine
-
pH 7.3, 37°C
0.22
N-acetyllactosamine
-
mutant enzyme N101Q, in citrate/phosphate buffer, pH 4.5, at 37°C
0.22
N-acetyllactosamine
-
mutant enzyme N101Q, at pH 4.5 and 37°C
0.27
N-acetyllactosamine
-
mutant enzyme N62Q, in citrate/phosphate buffer, pH 4.5, at 37°C
0.27
N-acetyllactosamine
-
mutant enzyme N62Q, at pH 4.5 and 37°C
0.3
N-acetyllactosamine
-
pH 6.5, 30°C, commercial FucT-VI
0.422
N-acetyllactosamine
pH 7.5, 37°C
0.61
N-acetyllactosamine
-
wild type enzyme, in citrate/phosphate buffer, pH 4.5, at 37°C
0.61
N-acetyllactosamine
-
recombinant wild type enzyme, at pH 4.5 and 37°C
0.2
NeuAcalpha(2,3)Galbeta(1,4)GlcNAc
-
-
0.9
NeuAcalpha(2,3)Galbeta(1,4)GlcNAc
-
pH 7.3, 37°C
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R115W/E116D
-
double mutation slightly increases H-type 1 activity
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
A128N
-
mutant obtained by focused directed evolution mutant, 3.4fold higher catalytic activity than wild-type
-
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
-
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
-
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
-
mutant enzyme is inactive
N101Q/N153Q
-
the mutations lead to an almost complete loss of enzymatic activity
N191Q/N153Q
-
the mutant almost completely loses enzymatic activity
A128N
-
the mutant displays 3.4fold higher catalytic activity with D-lactose than the wild type enzyme
A128N
mutant obtained by focused directed evolution mutant, 3.4fold higher catalytic activity than wild-type
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 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
-
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
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
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 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 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
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
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 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
-
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
-
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
-
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
-
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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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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a marked reduction in formation of metastatic foci is observed in FucT7 deficient mice injected with murine colon carcinoma cells MC-38GFP
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-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
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
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
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primary adhesion of Th1 lymphocytes obtained from FucT-VII deficient mice is drastically reduced
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Homo sapiens
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Homo sapiens
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Homo sapiens
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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.
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