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Enzyme Nomenclature
Information on EC 2.4.1.152 - 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase
Word Map on EC 2.4.1.152
- 2.4.1.152
-
sialylated
-
fucosylated
-
selectins
-
e-selectin
- fuc-tiii
-
fucts
- n-acetyllactosamine
- medicine
-
alpha1,3-fucosylation
-
1-3glcnac
- alpha-2-l-fucosyltransferase
-
sialyl-lex
-
selectin-dependent
- fuct-iv
-
lewisx
- synthesis
- drug development
- biotechnology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.4.1.152
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RECOMMENDED NAME
GeneOntology No.
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-beta-L-fucose + (1->4)-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R = GDP + (1->4)-beta-D-galactosyl-[alpha-(1->3)-L-fucosyl]-N-acetyl-D-glucosaminyl-R
i.e. Lewis X determinent
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:(1->4)-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-alpha-L-fucosyltransferase
Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. This enzyme fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4, unlike EC 2.4.1.65, 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase, which fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3.
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CAS REGISTRY NUMBER
COMMENTARY
111310-38-4
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39279-34-0
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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349722, 349723, 349725, 637640, 637641, 637642, 639518, 639519, 639520, 639521, 639522, 639526, 639527, 639528, 639530, 639531, 639532, 639533, 658281, 659454, 660698, 662063, 671207, 672496, 673753, 680959, 685736, 690403, 691805, 692533, 695068, 703540, 703902, 704786, 706697, 721501, 722371, 723313
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enzyme is produced by infection of Trichoplusia ni cells with recombinant baculovirus
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
suppression of isoform Fut10 expression induces the differentiation of neural stem cells and embryonic stem cells. In addition, knockdown of Fut10 expression in the cortical ventricular zone of the embryonic brain impairs the radial migration of neural precursor cells
metabolism
the enzyme is specifically responsible for Sialyl-Lewis X synthesis
physiological function
physiological function
-
synthesis of E- and P-selectin ligands, as mediated by the rate-limiting enzyme FucT-VII, plays an important role in the pathogenesis of atherosclerosis
physiological function
glycoproteins from tobacco line xFxG1, in which expression of a hybrid beta-(1-4)-galactosyltransferase and a hybrid a-(1-3)-fucosyltransferase IXa (FUT9a) is combined, contain an abundance of hybrid N-glycans with Lewis X (LeX) epitopes
physiological function
-
largest amount of recombinant FucT-IX is obtained in Sf9-insect cells by use of a baculovirus inducible protein production system
physiological function
-
protein kinase R is the primary target for Herpes simplex virus type 1 early RNA during induction of FUT3, FUT5, and FUT6, whereby the subsequent steps in the transcriptional activation of these host genes involve a hitherto unknown IMD-0354, yet IKK-2-independent, pathway
physiological function
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upregulation of selectin ligands in the endometrium at the time of implantation may be mediated, at least in part, by the regulation of FUT4 expression
physiological function
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overexpression of FUT6 in hepatocellular carcinoma cells enhance S-phase cell population, promoted cell growth and colony formation ability. FUT6 plays an important role in hepatocellular carcinoma cell growth by regulating the phosphatidyl inositol 3-kinase/Akt signaling pathway
physiological function
-
the enzyme plays a role in colorectal carcinoma metastases by promoting the carbohydration of glycoprotein CD24
physiological function
-
fucosyltransferase IV is implicated in the modulation of cell migration, invasion and cancer metastasis. The enzyme has a role in epithelial-mesenchymal transition through activation of the phosphatidylinositol 3-kinase/Akt and nuclear factor-kappaB signaling systems, which induce the key mediators Snail and MMP-9 and facilitate the acquisition of a mesenchymal phenotype
physiological function
-
overexpression of isoform Fut10 enhances the self-renewal of neural stem cells
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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-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 + N-acetyllactosamine
GDP + alpha1,3-fucosyl-N-acetyllactosamine
-
FucT-VI
-
-
?
GDP-beta-L-fucose + 4-deoxy-Galbeta1,4GlcNAc
?
-
8% of the activity with Galbeta1,4GlcNAc
-
-
?
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 + 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 + 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 + 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-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-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-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 + Galbeta1-4GlcNAcbeta1-2Manalpha1-6(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 + 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 + alpha(2,3)-sialyllactosamine
GDP + ?
-
115% of the activity with Galbeta(1,4)GlcNAc
-
-
?
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 + 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 + 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-O(CH2)8CO2CH3
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-O(CH2)8CO2CH3
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-neotetraose
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
-
-
-
?
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
-
-
-
?
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 + 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 + 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 + 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-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 + 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 + 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 + ?
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
?
-
-
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 specifity 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
?
-
-
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
?
-
-
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 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 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
?
-
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 specifity 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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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 + N-acetyllactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
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 + 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
-
-
-
-
?
additional information
?
-
Q49ME5
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q2VU44
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q32WF4
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q8UVZ3
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
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
?
-
P51993
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
?
-
Q495W5
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
?
-
Q5Q0U2
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
?
-
Q11131
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
?
-
Q2KQ71
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q70AG8
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q70AG9
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q70AH0
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q70AH1
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q70AH2
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q70AH3
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q70AH4
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q6WNG3
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
additional information
?
-
Q49ME6
evolution of vertebrate alpha-1,3/4-fucosyltransferases
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
Zn2+
additional information
-
CEFT-3 does not require divalent cations, while CEFT-4 is activates by some divalent cations, with slight prefernce for Ca2+
Mn2+
-
acts as electrophilic catalyst in the nonenzymatic hydrolysis of GDP-fucose
Mn2+
-
1.9-fold increase in activity at Mn2+ concentrations between 2.5 and 10 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-ethynylnaphthalene
-
exhibits highly potent inhibitory effects against the FUT-VI mediated sialyl Lewis X synthesis
deoxyfuconojirimycin
-
modest inhibitor, causes 21% inhibition, synergism: combined with GDP at their Ki levels results in 80% inhibition, combined with GMP causes 50.4% inhibition
GDP-(1-[2-[(naphthalen-1-ylmethyl)-carbamoyl]-ethyl]-1H-[1,2,3]triazol-4-ylmethyl)
-
-
GDP-[1-[3-(1,2-diphenyl-ethylcarbamoyl)-butyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
GDP-[1-[3-(1,2-diphenyl-ethylcarbamoyl)-propyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
GDP-[1-[4-(9,10-dioxo-9,10-dihydro-anthracen-2-ylcarbamoyl)-butyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
L-fucal
-
modest inhibitor, causes 26% inhibition, combined with GDP causes 40% inhibition
-
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta-biphenyl-4-carboxylic acid propyl amide
-
-
tunicamycin
inhibits N-glycosylation of the enzyme in recombinant COS-7 cells which leads to inactivation of rFuc-TVII
diethyldicarbonate
-
IC50: 0.092. Preincubation at 23°C gives maximal inhibition, 75%, after 180 s. Preincubation at 13°C gives 55% inhibition after 3 min. Preincubation at 4°C results in only 35% inhibition
GDP
-
0.191 mM causes 50% inhibition in the scintillation proximity assay and 0.214 mM causes 50% inhibition in the Dowex assay
NEM
-
50% inhibition at 0.1 mM, complete inhibition at 0.5 mM. At 37°C complete inhibition is reached after 3 min. At 23°C more than 10 min are required to reach maximal activity. No inactivation after 10 min at 4°C
NEM
-
activity in HL-60 cells is essentially unaffected. The RPMI 8226 enzyme activity is significantly inhibited
NEM
-
recombinant fusion protein of protein A coupled to the catalytic domain of FucT-V, irreversible inactivation, effective protection by GDP-fucose and GDP
additional information
-
CEFT-3 acts optimally in the presence of EDTA/EGTA, indicating that cations inhibit this activity
-
additional information
-
development of a high-throughput screening system for identification of FucT-VII inhibitors utilizing scintillation proximity assay with fetuin-coated beads, overview
-
additional information
-
incubation with anti-Lex monoclonal antibody L5 leads to impaired adhesion of NT2N neurons to the surface matrix and inhibits neurite initiation
-
additional information
-
high-throughput screening for FucTVII inhibitors, overview
-
additional information
-
inhibitor synthesis and FRET-based inhibition assay analysis, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
interleukin-6 or interleukin-8 significantly induce the expression of alpha1,3/4-fucosyltransferases, the amounts of sialyl-Lewisx and 6-sulfo-sialyl-Lewisx epitopes at the periphery of high molecular-mass proteins, including MUC4, are increased
-
additional information
-
FucT-IX-MBP fusion protein is soluble but catalytically inactive. From the culture supernatant of Sf9-insect cells, which constitutively produce recombinant FucT-IX, is obtained soluble protein with an enzymatic activity of approximately 250 mU/l after three days of cultivation, the level of activity differs depending on the type of signal sequence and the position of the tag. The melittin signal sequence and N-terminal tags result in the highest enzymatic activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
0.021
GDP-beta-fucose
-
pH 6.5, 30°C, recombinant FucT-VII and commercial FucT-VI
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
-
-
0.19
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
-
-
0.25
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
-
-
0.05
Neu5Acalpha(2,3)-Galbeta(1,4)-6-O-sulfo-GlcNAc beta-O-C3H6-biotin
-
pH 7.4, 22°C
0.39
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1–441)
1.7
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1–428)
0.0026
GDP-beta-L-fucose
-
recombinant wild type enzyme, at pH 4.5 and 37°C; wild type enzyme, 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; mutant enzyme N101Q, in citrate/phosphate buffer, pH 4.5, at 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(1–441)
0.0176
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1–428)
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
0.37
GDP-beta-L-fucose
-
mutant enzyme A128N, at pH 7.6 and 37°C; mutant enzyme A128N/H129E, at pH 7.6 and 37°C
0.22
N-acetyllactosamine
-
mutant enzyme N101Q, at pH 4.5 and 37°C; mutant enzyme N101Q, in citrate/phosphate buffer, pH 4.5, at 37°C
0.27
N-acetyllactosamine
-
mutant enzyme N62Q, at pH 4.5 and 37°C; mutant enzyme N62Q, 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; wild type enzyme, in citrate/phosphate buffer, pH 4.5, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.97
D-lactose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
1.1
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1–428)
2.3
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1–428)
0.478
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I, at pH 7.6 and 37°C
1.1
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1–428)
1.328
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/S46F, at pH 7.6 and 37°C
1.512
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
2.3
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1–428)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.083
D-lactose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
1.992
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I, at pH 7.6 and 37°C
4.742
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/S46F, at pH 7.6 and 37°C
5.041
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000901
GDP-(1-[2-[(naphthalen-1-ylmethyl)-carbamoyl]-ethyl]-1H-[1,2,3]triazol-4-ylmethyl)
-
-
0.000437
GDP-[1-[(1,2-diphenyl-ethylcarbamoyl)-methyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
0.000376
GDP-[1-[3-(1,2-diphenyl-ethylcarbamoyl)-butyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
0.001069
GDP-[1-[3-(1,2-diphenyl-ethylcarbamoyl)-propyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
0.000511
GDP-[1-[4-(9,10-dioxo-9,10-dihydro-anthracen-2-ylcarbamoyl)-butyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.092
diethyldicarbonate
Homo sapiens
-
IC50: 0.092 mM. Preincubation at 23°C gives maximal inhibition, 75%, after 180 s. Preincubation at 13°C gives 55% inhibition after 3 min. Preincubation at 4°C results in only 35% inhibition
0.035
Neu5(OHAc)alpha(2-3)Galbeta(1-4)GlcNAc-beta-(3-amino)propyl
Homo sapiens
-
pH 7.4, 22°C
0.0838
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta(1-3)LacN-(2-acetamido)ethyl
Homo sapiens
-
pH 7.4, 22°C
0.0347
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta(1-6)GalNAc-(2-acetamido)ethyl
Homo sapiens
-
pH 7.4, 22°C
0.0143
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta-biphenyl-4-carboxylic acid propyl amide
Homo sapiens
-
pH 7.4, 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
measurement of alpha(1-3)fucosyltransferase activity using scintillation proximity
additional information
-
assay development utilizing anion exchange chromatography, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
6.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.8
-
pH 6.0: about 40% of maximal activity, pH 8.8: about 50% of maximal activity, reaction with N-acetyllactosamine
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
22
22
-
optimal enzyme activity at room temperature, rapid loss of activity at 37°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 50
4 - 50
4°C: 90% of maximal activity, 50°C: over 40% of maximal activity
4 - 50
temperature range for FucTC is very broad, enzyme shows 90% of maximal activity at 4°C and 40% of maximal activity at 50°C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
FUT7 mRNA minorly expressed in mouse brain endothelial cell line bEND.3
-
the enzyme is expressed in endothelial cells lining the high endothelial venules of perpheral lymph nodes, mesenteric lymph nodes and Pever‘s patches
-
FT-IV mRNA is the predominant transcript in eosinophils isolated from human blood, TGF-beta1 upregulates FT-IV mRNA expression; FT-VII mRNA is weakly expressed in eosinophils isolated from human blood, its expression is up-regulated by TGF-beta1 to some extent
-
FUT4 mRNA is prominently expressed in Jurkat cells, a human T cell line, FUT4 and FUT9 mRNA are distinctly up-regulated in Jurkat cells 3 h and 12 h after granzyme B treatment, respectively, whereas other FUT mRNAs are not affected; FUT9 mRNA is scarcely expressed in Jurkat cells, a human T cell line, FUT4 and FUT9 mRNA are distinctly up-regulated in Jurkat cells 3h and 12 h after granzyme B treatment, respectively, whereas other FUT mRNAs are not affected
rFuc-TVII mRNA expression strongly detected in rat lymph node
-
FUT7 mRNA remarkably highly expressed in mouse lymphoid tumor cell line TIB-63
-
FUT7 mRNA significantly expressed in mouse macrophage cell line TIB-69
NTERA-2/cl.D1 cells are cultured and differentiated into NT2N neurons
additional information
-
in individuals with plasma fucosyltransferase deficiency from Indonesia, either a missense mutation, G739A, in the catalytic domain, or a nonsense mutation, C945A, truncating the COOH terminus of the enzyme, leads to the total loss of the enzymatic activity of FUT6. 9% of individuals on the island of Java lack the plasma type enzyme. Activity is elevated in patients with a variety of malignant disorders, including liver cancer, elevated in heavy alcohol drinkers. Reduction of enzyme level in patients with schizophrenia
-
enzyme activity is significantly higher in patients with chronic liver diseases than in that of normal controls
-
during renal organogenesis the myeloid enzyme is progressively replaced by the plasma enzyme in the proximal tubules and later by the Lewis enzyme in Bellini‘s ducts and calyce
rFuc-TVII mRNA expression undetectable in kidney but it is strongly enhanced during acute inflammatory reaction induced by kidney allograft rejection
-
FUT7 mRNA expression is highly up-regulated in rat kidney allograft 3 to 5 days after transplantation
additional information
-
developmental expression of CEFT isozymes, overview
additional information
-
enzyme is produced by infection of Trichoplusia ni cells with recombinant baculovirus
additional information
-
recombinant enzyme expressed in Sf-9 cells via baculovirus infection
additional information
-
no activity detected in Daudi, Raji and Reh leukemia cells
additional information
-
throughout the menstrual cycle, FUT4 protein is localized to glandular and luminal epithelium in the endometrium
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
hsp150delta-FucTe fusion protein remains mostly non-covalently attached to the cell wall
-
the enzyme possesses a cytoplasmic domain, a transmembrane domain, and a Golgi lumenal catalytic domain
-
type II membrane protein, membrane-bound form in trans cistermae of Golgi
-
; type II membrane protein, membrane-bound form in trans cistermae of Golgi
type II membrane protein, membrane-bound form in trans cistermae of Golgi; type II membrane protein, membrane-bound form in trans cistermae of Golgi
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
41000
44000
47000
51200
-
x * 51200, alpha-(1,3/1,4)-fucosyltransferase(1-428), calculated from sequence; x * 51200, mutant alpha-(1,3/1,4)-fucosyltransferase (1–441), calculated from sequence
54000
-
x * 54000, glycosylated FUT9, SDS-PAGE, x * 47000, deglycosylated FUT9, SDS-PAGE
39000
-
x * 39000, wild-type enzyme, SDS-PAGE, x * 44000-46000, recombinant FucT-VII catalytic domain-protein A fusion protein, SDS-PAGE
41000
-
x * 41000, fully glycosylated His-tagged enzyme, SDS-PAGE; x * 41000, recombinant enzyme, SDS-PAGE
47000
-
x * 54000, glycosylated FUT9, SDS-PAGE, x * 47000, deglycosylated FUT9, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
the enzyme possesses a cytoplasmic domain, a transmembrane domain, and a large Golgi lumenal catalytic domain
?
-
x * 38000, SDS-PAGE; x * 39000, calculated from amino acid sequence
-
?
-
x * 51200, alpha-(1,3/1,4)-fucosyltransferase(1-428), calculated from sequence; x * 51200, mutant alpha-(1,3/1,4)-fucosyltransferase (1–441), calculated from sequence
?
-
x * 51200, alpha-(1,3/1,4)-fucosyltransferase(1-428), calculated from sequence; x * 51200, mutant alpha-(1,3/1,4)-fucosyltransferase (1–441), calculated from sequence
-
?
-
x * 51200, alpha-(1,3/1,4)-fucosyltransferase(1-428), calculated from sequence; x * 51200, mutant alpha-(1,3/1,4)-fucosyltransferase (1–441), calculated from sequence
-
?
-
x * 39000, wild-type enzyme, SDS-PAGE, x * 44000-46000, recombinant FucT-VII catalytic domain-protein A fusion protein, SDS-PAGE
?
-
x * 54000, glycosylated FUT9, SDS-PAGE, x * 47000, deglycosylated FUT9, SDS-PAGE
?
-
x * 41000, fully glycosylated His-tagged enzyme, SDS-PAGE; x * 41000, recombinant enzyme, SDS-PAGE
monomer
1 * 41892, calculation from nucleotide sequence; 1 * 43034, calculation from nucleotide sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
FUT9 is a type II membrane protein with three potential N-glycosylation sites
glycoprotein
-
the enzyme contains three potential N-glycosylation sites (Asn-XSer/Thr, X is any amino acid except proline) at amino acid positions 62, 101 and 153, respectively; the enzyme contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153)
glycoprotein
Tyr191 of rFuc-TVII is predicted to be O-glycosylated, three potential N-glycosylation sites at residues 86, 109, and 299, N-glycosylation is necessary for enzymatic activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilized alpha-(1,3/1,4)-fucosyltransferase(1-428) loses 23% of its activity after 3 month
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilized alpha-(1,3/1,4)-fucosyltransferase(1–441) loses 38% activity after 3 months
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; alpha-(1,3/1,4)-fucosyltransferase(1–428) with a His6 tag at the C terminus is purified
-
native enzyme by preparation of microsome and Golgi membrane fractions, ultracentrifugation, and affinity chrotography
-
recombinant FucT-VII catalytic domain-protein A fusion protein from Sf21 insect cells by IgG affinity chromatography
-
using ammonium sulfate precipitation, hydrophobic chromatography in phenyl-Sepharose, ion-exchange chromatography on sulfopropyl-Sepharose, affinity chromatography on GDP-heanolamine-Sepharose, and finally high pressure liquid chromatography gel filtration
-
using method A: column chromatography on DEAE-Sephadex, SP-Sephadex, ASTD-Sepharose and GTP-Agarose, method B: column chromatography on DEAE-Sephacel, SP-Sephadex and Synsorb-Galbeta1-4GlcNAc
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; full-length and each truncated FucT (DELTAFucT) are expressed in Escherichia coli HMS174DE3
-
applying a baculovirus system in Spodoptera frugiperda Sf9 cells; expressed in Sf9 insect cells
-
CEFT DNA and amino acid sequence determination and analysis, expression analysis, expression in COS-7 cells
-
cloning of rat Fuc-TVII gene which is expressed as two splice variants, but only the long one shows enzymatic activity, expression of the long splice variant in COS-7 cells
expressed in COS-1 cells
expression in CHO cells, to confirm the hypothesis that FucT-VII and keratin sulfate sulfotransferase (KSST) may compete for the same acceptor molecules FucT-VII and Core2GlcNAcT-1 are expressed in CHO cells stably expressing KSST, sialyl Lewis X expression is significantly reduced in these cells
-
expression in CHO cells; poly-LDN backbone is efficiently fucosylated by recombinant human alpha1,3-fucosyltransferase IX (FucT 9) when it is stably co-expressed with the Cebeta4GalNAcT in cell line L8-GalNAcT-FucT
-
expression in hepatocellular carcinoma H7721 cells, alpha1,3FucT-VII acts as a potential antiapoptotic factor in H7721 cells after induction of apoptosis by UV irradiation, increasing phosphorylated JNK, quantitative real-time PCR analysis of expression of enzyme product SLex, overview
-
expression in Pichia pastoris GS115 cells; expression in Sf9 cells; the Apis mellifera genome encodes three alpha1,3-FucT homologues FucTA, FucTB and FucTC, expressed in yeast and insect cells only FucTA is found to be a core alpha1,3-FucT (EC 2.1.214), FucTC discloses to be the first Lewis-type alpha1,3-FucT (EC 2.4.1.152) to be described in insects, FucTB does not show any activity
FucT-VII-/-GFP+ bone marrow transplanted into lethally irradiated low-density lipoprotein receptor low density lipoprotein receptor mice or FucT-VII+/+GFP+ bone marrow into FucT-VII-/-, low density lipoprotein receptor double-mutant mice
-
FucT-VII: DNA and amino acid sequence determination and analysis, expression of the catalytic domain of FucT-VII fused to protein A from Staphylococcus aureus in Spodoptera frugiperda Sf21 insect cells via the baculovirus infection system
-
full-length form of human FUT9 and a truncated form containing sFUT9 the catalytic domain of the enzyme are overexpressed in Spodoptera frugiperda (Sf9) insect cells using the signal sequence of human interleukin 2 for efficient secretion, high activity of the trunctated, soluble form sFUT9 in the supernatant of Sf9 cells, sFUT9 fucosylates sialylated and non-sialylated glycoproteins
-
fusion construct consisting of maltose-binding protein and soluble FucT-IX overexpressed in Escherichia coli. Constitutive expression of FucT-IX in Sf9 insect cells, different recombinant baculoviruses containing the N-terminal signal sequences from gp67and beta-trace proteins followed by a histidine tag fused to the soluble FucT-IX-encoding sequence, respectively, and infection of Sf9 cells
-
FUT9, DNA and amino acid sequence determination and analysis, transient overexpression of His-tagged or V5-tagged wild-type and mutant FUT9 proteins in HeLa cells
-
gene fragment encoding the catalytic domain comprising residues 38–359 of FUT9a fused N-terminally with the sequence encoding the first 53 aa of the Arabidopsis thaliana XylT gene. Hybrid gene placed under control of the Cassava Vein Mosaic virus promoter, and the resulting expression cassette combined with the one comprising the hybrid GalT under control of the CaMV 35S promoter. Transferred to a plant transformation vector conferring hygromycin resistance, which is designated xFxG
gene FUT11, expression analysis in bronchial mucosa of cystic fibrosis patients
-
overexpression in A-431 cells cells, two stable FUT-4 cell lines A431-FUT4-1 and A431-FUT4-2
-
putative cDNA amplified by PCR from a cDNAlambdaZAP library, cloned into the mammalian expression vector pCR3.1 and sequenced, transfection of COS7 kidney cells from the African green monkey with cDNA encoding the enzyme results in about 20fold level of activity over control cells, using lacto-N-neotetraose as acceptor
-
regions 5' of the FUT VI transcription start site, -2,067 to +1 nt and -2,067 to +213 nt isolated, PCR products 5'-phosphorylated using the T4 polynucleotide kinase and then ligated into pGL4.11 vector digested with EcoRV and treated with alkaline phosphatase from Escherichia coli. Plasmids transiently transfected into HepG2 and HuH-7 cells
-
truncated constructs lacking the transmembrane region and the cytosolic N-terminus, are expressed in baculovirus-infected Trichoplusia ni insect cells and in two non-lytic expression systems, stably transfect human HEK 293 and Trichoplusia ni cells. Since secretion of some glycosyltransferases is controlled by formation of dimeric molecules via disulfide bonds, one of the fucosyltransferase V constructs contains the N-terminal cysteine residue 64 for dimerization, whereas this residue is replaced in the other construct by serine
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
FUT4 mRNA is significantly upregulated during the early and midsecretory stages of the menstrual cycle compared with the other menstrual phases, with maximal expression during the mid-secretory phase. In proliferative explants, progesterone significantly increases FUT4 transcription and translation after 24 h in culture. Estrogen does not have any significant effects
-
FUT4 staining is weak in proliferative and menstrual endometrium. Inductive effect of progesterone on FUT4 transcription is lost after 48 h of treatment
-
higher mRNA and protein expression of the enzyme are observed in colorectal tumors compared with adjacent normal ones
-
in hepatocellular carcinoma tissues, the expression levels and activity of alpha1,3/4-fucosyltransferase FUT6 are significantly up-regulated
-
protein kinase R function is essential for FUT3, FUT5, and FUT6 induction and sLex expression in Herpes simplex virus type 1-infected cells. IMD-0354, an inhibitor of the NF-kappaB-activating factor IKK-2, induces FUT transcription via a IKK-2-independent mechanism, irrespective of whether the cells are virus-infected or not
-
protein kinase R inhibitors 2-aminopurine and C16 inhibit FUT3, FUT5, and FUT6 expression. MG-132 inhibits the IMD-0354-dependent transcription of FUT5 in a dose-dependent manner
-
two hepatocyte nuclear factor-4alpha (HNF-4alpha) and one octamer binding transcription factor-1 (Oct-1) binding sites are essential for FUT VI transcription, which are the 5'-flanking regions at positions -156 to -136 nt and -56 to -19 nt relative to the FUT VI gene transcription start site. Transient overexpression of HNF-4alpha but not Oct-1 enhances both FUT VI promoter activities and FUT VI mRNA levels in HuH-7 cells. FUT VI mRNA levels are higher in HepG2 cells than in HNF-4alpha-transfected HuH-7 cells
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
-
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
N101Q
-
the mutant shows about 30% of wild type activity; the mutant still shows about 27% of wild type activity
N101Q/N153Q
-
the mutations lead to an almost complete loss of enzymatic activity
N153Q
-
the mutant almost completely loses enzymatic activity; the mutation leads to an almost complete loss of enzymatic activity
N62Q
-
the mutant shows about 60% of wild type activity; the mutant still shows about 62% of wild type activity
N62Q/N101Q
-
the mutant almost completely loses enzymatic activity; the mutations lead to an almost complete loss of enzymatic activity
N62Q/N153Q
-
the mutant almost completely loses enzymatic activity; the mutations lead to an almost complete loss of enzymatic activity
additional information
additional information
-
with full length 11639FucT, 28% of total enzyme activities is localized in the soluble fraction. For alpha-(1,3/1,4)-fucosyltransferase(1–441), 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(10–447) completely loses activity; 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(1–441), 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(10–447) completely loses activity; 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(1–441), 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(10–447) completely loses activity; 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
-
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; 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
-
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
double knock-out mice deficient for both FT-IV and FT-VII show an essential absence of eosinophil recruitment to the dermis; double knock-out mice deficient for both FT-IV and FT-VII show an essential absence of eosinophil recruitment to the dermis; FT-IV deficient mice show a significant decrease in eosinophil recruitment to the skin; FT-VII deficient mice show a decrease in eosinophil recruitment to the skin
additional information
-
a marked reduction in formation of metastatic foci is observed in FucT7 deficient mice injected with murine colon carcinoma cells MC-38GFP
additional information
-
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
-
primary adhesion of Th1 lymphocytes obtained from FucT-VII deficient mice is drastically reduced
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
a baculoviral expression system of FucT-IX appears to be a promising strategy for overproduction as compared to overproduction in Escherichia coli or mammalian cells
drug development
medicine
synthesis
drug development
-
development of a high-throughput screening system for identification of FucT-VII inhibitors, which could have anti-inflammatory or anti-metastatic potential, utilizing scintillation proximity assay with fetuin-coated beads, overview
drug development
-
fucosyltransferase VII is a very promising drug target for treatment of inflammatory skin diseases
drug development
-
FucT-VII and the E- and P-selectin pathways may prove a fruitful therapeutic target in the prevention or treatment of atherosclerosis
medicine
-
FUT7 mRNA is highly over-expressed at the site of inflammation and in tumorigenesis
medicine
-
FUT7 mRNA is highly over-expressed at the site of inflammation and in tumorigenesis
medicine
FT-IV and FT-VII are both important contributors to selectin-dependent eosinophil recruitment to the skin and may represent therapeutic targets in which eosinophil recruitment contributes to pathophysiology; FT-IV and FT-VII are both important contributors to selectin-dependent eosinophil recruitment to the skin and may represent therapeutic targets in which eosinophil recruitment contributes to pathophysiology
medicine
-
granzyme B-induced caspase 3-activation leads to up-regulation of FUT4 and FUT9 mRNA expression, which increases the surface expression of Lewis X and Y antigens
medicine
-
FucT-VII is critical for the recruitment of Th1 cells in inflamed brain microcirculation
medicine
-
fucosyltransferase IV overexpression promotes cell proliferation, increases the expression of proliferating cell nuclear antigen and augments Lewis Y expression to trigger neoplastic cell proliferation, fucosyltransferase IV may serve as a potential therapeutic target for the treatment of Lewis Y-positive epithelial cancers
medicine
-
isoform FUT4 is a regulator of epithelial-mesenchymal transition in breast cancer cells and a target for cancer therapy
synthesis
-
stable expression of beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans and human FucT9 in CHO cells, producing fucosylated poly-LacdiNAc N-glycans
synthesis
-
recombinant yeast cells which provide an inexpensive, self-perpetuating source of fucosyltransferase activity immobilized in the cell wall, useful for in vitro synthesis of sLex
synthesis
a chemoenzymatic model for the preparative-scale synthesis of a diverse array of GDP-fucose derivatives is reported
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