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Information on EC 2.4.1.152 - 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase and Organism(s) Homo sapiens and UniProt Accession P51993
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2.4.1.152 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferaseIUBMB Comments
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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Word Map
- 2.4.1.152
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sialylated
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fucosylated
- selectins
- fuc-tiii
- n-acetyllactosamine
- medicine
- synthesis
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alpha1,3-fucosylation
- lewisx
- fuc-ts
- fuct-iv
- alpha-2-l-fucosyltransferase
- analysis
- drug development
- biotechnology
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
fuc-tv, alpha-3-fucosyltransferase, fucosyltransferase 4, alpha-3-l-fucosyltransferase, alpha1,3 fuct-vii, fut vi, alpha1,3ft, alpha1,3-fuct, fucosyltransferase-vii, fucosyltransferase ix, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha(1-3)fucosyltransferase
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alpha-3-fucosyltransferase
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alpha-3-L-fucosyltransferase
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alpha1,3 fucosyltransferase
alpha1,3FT
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alpha1-3 fucosyltransferase
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alpha1->3fucosyltransferase
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alpha3-fucosyltransferase-V
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alpha3-fucosyltransferase-VI
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Fuc-Tb
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Fuc-TV
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fucosyltransferase 11
fucosyltransferase, guanosine diphosphofucose-glucoside alpha1-->3-
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FucT-VI
FUT4
FUT5
FUT6
FUT7
Fut9
galactoside 3-fucosyltransferase
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GDL-L-fucose:N-acetyl-beta-D-glucosaminyl alpha-3-L-fucosyltransferase
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GDP-Fuc:Galbeta1-4GlcNAc (Fuc to GlcNAc) alpha1-3 fucosyltransferase
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GDP-fucose:beta-D-N-acetylglucosaminide 3-alpha-fucosyltransferase
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GDP-fucose:Galbeta(1-4)GlcNAc-R alpha(1-3)fucosyltransferase
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GDP-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-galactosaminyl-R 3-L-fucosyltransferase
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guanosine diphosphofucose glucoside alpha1->3fucosyltransferase
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lewis-negative alpha-3-fucosyltransferase
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plasma alpha-3-fucosyltransferase
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alpha1,3 fucosyltransferase
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FucT-VI
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FUT5
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FUT6
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R 3-alpha-L-fucosyltransferase (configuration-inverting)
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.
CAS REGISTRY NUMBER
COMMENTARY
111310-38-4
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39279-34-0
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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
-
-
?
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-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 + asialo-erythropoietin
?
wild-type FUT9 efficiently fucosylates di-, tri- and tetraantennary N-glycans from asialoEPO
-
-
?
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-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
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sialyl-Lewisx terminal structure
-
-
?
GDP-fucose + (-3GalNAcbeta1-4GlcNAcbeta1-)n
GDP + (-3GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-)n
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N-glycans containing poly-LDN structures are efficiently fucosylated by human FucT9 producing poly-LDNF structures, max. 4-6 repeating LDNF units
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?
GDP-fucose + asialo human erythropoietin
GDP + fucosylated asialo human erythropoietin
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-
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?
GDP-fucose + bovine asialofetuin
GDP + fucosylated bovine asialofetuin
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-
-
?
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc-O-(CH2)3NHCO(CH2)5-biotin
-
-
-
-
?
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAcbeta1-R
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-R
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Lewis Y antigen, increased expression in cancer cells
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?
GDP-fucose + Galbeta(1,3)GlcNAcOMe
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcOMe
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-
-
-
?
GDP-fucose + Galbeta1-4Glc-NAc-O-(CH2)3NHCO(CH2)5-NH-biotin
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
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-
-
-
?
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 + GalNAcbeta1-4GlcNAcbeta-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
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-
-
-
?
GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-acetylamino-beta-D-glucopyranose
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-acetylamino-beta-D-glucopyranose
-
-
-
-
?
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 + 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 + 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)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)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 + 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-fucose + Fucalpha1-2Galbeta1-4GlcNAc
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc
-
-
-
?
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAc
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc
-
-
-
?
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 + 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
?
-
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
?
-
-
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
?
-
-
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
-
-
-
NATURAL SUBSTRATE
NATURAL 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
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 + 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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
Zn2+
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
INHIBITOR
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
-
-
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
-
development of a high-throughput screening system for identification of FucT-VII inhibitors utilizing scintillation proximity assay with fetuin-coated beads, overview
-
additional information
-
high-throughput screening for FucTVII inhibitors, 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
-
incubation with anti-Lex monoclonal antibody L5 leads to impaired adhesion of NT2N neurons to the surface matrix and inhibits neurite initiation
-
additional information
-
inhibitor synthesis and FRET-based inhibition assay analysis, overview
-
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
-
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
0.0026
GDP-beta-L-fucose
-
wild type enzyme, in citrate/phosphate buffer, pH 4.5, at 37°C
0.0047
GDP-beta-L-fucose
-
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
0.22
N-acetyllactosamine
-
mutant enzyme N101Q, in citrate/phosphate buffer, pH 4.5, at 37°C
0.27
N-acetyllactosamine
-
mutant enzyme N62Q, in citrate/phosphate buffer, pH 4.5, at 37°C
0.61
N-acetyllactosamine
-
wild type enzyme, in citrate/phosphate buffer, pH 4.5, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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]
-
-
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
-
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
-
during renal organogenesis the myeloid enzyme is progressively replaced by the plasma enzyme in the proximal tubules and later by the Lewis enzyme in Bellinis ducts and calyce
NTERA-2/cl.D1 cells are cultured and differentiated into NT2N neurons
-
NTERA-2/cl.D1 cells are cultured and differentiated into NT2N neurons
additional information
-
enzyme is produced by infection of Trichoplusia ni cells with recombinant baculovirus
additional information
-
no activity detected in Daudi, Raji and Reh leukemia cells
additional information
-
recombinant enzyme expressed in Sf-9 cells via baculovirus infection
additional information
-
throughout the menstrual cycle, FUT4 protein is localized to glandular and luminal epithelium in the endometrium
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
-
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
-
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
-
following FUT7 siRNA transfection, the expression of FUT7 is markedly downregulated. The synthesis of sialyl-Lewisx epitope is also inhibited, consistent with the downregulated expression of FUT7. MHCC-97 cell proliferation is also significantly inhibited following FUT7 siRNA transfection, which is correlated with suppression of the S-phase in cell cycle progression. The knockdown of FUT7 inhibits the activation of phospholipase Cgamma by inhibiting its translocation and phosphorylation
physiological function
-
FUT7 overexpression significantly promotes monocyte-endothelial adhesion, while FUT7 knockdown inhibits IL-1beta-induced monocyte-endothelial adhesion. Fucosylation of selectin ligand endomucin is directly involved in IL-1beta-induced monocyte-endothelial adhesion. p38 and extracellular signal-regulated kinase (ERK) MAPK signaling pathway are activated by IL-1beta, while inhibition of the p38/ERK signaling pathway decreases FUT7 expression level and IL-1beta-induced monocyte-endothelial adhesion
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FUT6_HUMAN
359
0
41860
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
-
x * 39000, wild-type enzyme, SDS-PAGE, x * 44000-46000, recombinant FucT-VII catalytic domain-protein A fusion protein, SDS-PAGE
41000
43008
44000
47000
x * 54000, glycosylated FUT9, SDS-PAGE, x * 47000, deglycosylated FUT9, SDS-PAGE
54000
x * 54000, glycosylated FUT9, SDS-PAGE, x * 47000, deglycosylated FUT9, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
additional information
-
the enzyme possesses a cytoplasmic domain, a transmembrane domain, and a large Golgi lumenal catalytic domain
?
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
FUT9 is a type II membrane protein with three potential N-glycosylation sites
glycoprotein
-
FUT9 is a type II membrane protein with three potential N-glycosylation sites
glycoprotein
-
the enzyme contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153)
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
N101Q/N153Q
-
the mutations lead to an almost complete loss of enzymatic activity
N153Q
N62Q
N62Q/N101Q
N62Q/N153Q
additional information
N62Q/N101Q
-
the mutations lead to an almost complete loss of enzymatic activity
N62Q/N153Q
-
the mutations lead to an almost complete loss of enzymatic 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
additional information
-
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
-
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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 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
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
-
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
-
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
-
the mRNA and protein expression levels of FUT7 are high in the MHCC-97 cell line compared with levels in normal liver cells
-
treatment with inflammatory factors interleukin-1beta pronouncedly upregulates alpha1,3-fucosyltransferase VII gene (FUT7) mRNA and protein expression level in EA.hy926 endothelial cells
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
synthesis of fluorescein-isothiocyanate-labeled and carboxyfluorescein-labeled NDP-beta-L-fucose derivatives, and application in labeling of different glycoproteins with the aid of fucosyltransferases. The fluorescein-isothiocyanate-labeled fucose is the best of these substrates, and the bacterial enzyme FucT tolerates the fluorescent substrates better than human fucosyltransferases
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
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
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
-
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
-
stable expression of beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans and human FucT9 in CHO cells, producing fucosylated poly-LacdiNAc N-glycans
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Foster, C.S.; Gillies, D.R.B.; Glick, M.C.
Purification and characterization of GDP-L-Fuc-N-acetyl-beta-D-glucosaminide alpha1,3 fucosyltransferase from human neuroblastoma cells. Unusual substrate specificities of the tumor enzyme
J. Biol. Chem.
266
3526-3531
1991
Homo sapiens
Sarnesto, A.; Kohlin, T.; Hindsgaul, O.; Vogele, K.; Blaszczyk-Thurin, M.; Thurin, J.
Purification of the beta-N-acetylglucosaminide alpha 1,3-fucosyltransferase from human serum
J. Biol. Chem.
267
2745-2752
1992
Homo sapiens
Murray, B.W.; Takayama, S.; Schultz, J.; Wong, C.H.
Mechanism and specificity of human alpha-1,3-fucosyltransferase V
Biochemistry
35
11183-11195
1996
Homo sapiens
Legault, D.J.; Kelly, R.J.; Natsuka, Y.; Lowe, J.B.
Human alpha(1,3/1,4)-fucosyltransferases discriminate between different oligosaccharide acceptor substrates through a discrete peptide fragment
J. Biol. Chem.
270
20987-20996
1995
Homo sapiens
Holmes, E.H.; Yen, T.Y.; Thomas, S.; Joshi, R.; Nguyen, A.; Long, T.; Gallet, F.; Maftah, A.; Julien, R.; Macher, B.A.
Human alpha1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites
J. Biol. Chem.
275
24237-24245
2000
Homo sapiens
Dupuy, F.; Germot, A.; Marenda, M.; Oriol, R.; Blancher, A.; Julien, R.; Maftah, A.
alpha1,4-Fucosyltransferase activity: a significant function in the primate lineage has appeared twice independently
Mol. Biol. Evol.
19
815-824
2002
Homo sapiens, Macaca mulatta
Weston, B.W.; Nair, R.P.; Larsen, R.D.; Lowe, J.B.
Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities
J. Biol. Chem.
267
4152-4160
1992
Homo sapiens (Q11128)
Vo, L.; Lee, S.; Marcinko, M.C.; Holmes, E.H.; Macher, B.A.
Human alpha1,3/4-fucosyltransferases II. A single amino acid at the COOH terminus of FucT III and V alters their kinetic properties
J. Biol. Chem.
273
25250-25255
1998
Homo sapiens
Cameron, H.S.; Szczepaniak, D.; Weston, B.W.
Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms
J. Biol. Chem.
270
20112-20122
1995
Homo sapiens (P51993), Homo sapiens (Q11128)
Johnson, P.H.; Yates, A.D.; Watkins, W.M.
Human salivary fucosyltransferases: evidence for two distinct alpha-3-L-fucosyltransferase activities one or which is associated with the Lewis blood group Le gene
Biochem. Biophys. Res. Commun.
100
1611-1618
1981
Homo sapiens
Johnson, P.H.; Watkins, W.M.
Sialyl compounds as acceptor substrates for human alpha-3- and alpha-3/4-L-fucosyltransferases
Biochem. Soc. Trans.
13
1119-1120
1985
Homo sapiens
-
Johnson, P.H.; Watkins, W.M.
Separation of an alpha3-L-fucosyltransferase from the blood-group-Le-gene specified alpha-3/4-L-fucosyltransferase in human milk
Biochem. Soc. Trans.
10
445-446
1982
Homo sapiens
-
Prieels, J.P.; Beyers, T.; Hill, R.L.
Human milk fucosyltransferase
Biochem. Soc. Trans.
5
838-839
1977
Homo sapiens
Kannagi, R.
alpha3-Fucosyltransferase-VI (FUT6)
Handbook of Glycosyltransferases and Related Genes; (Taniguchi, N. ; Honk, K. ; Fukuda, M. , eds. )
237-245
2002
Bos taurus, Homo sapiens
-
Kannagi, R.
alpha3-Fucosyltransferase-V (FUT5)
Handbook of Glycosyltransferases and Related Genes; (Taniguchi, N. ; Honk, K. ; Fukuda, M. eds.)
232-236
2002
Cricetulus griseus, Homo sapiens
-
Hood, C.M.; Kelly, V.A.; Bird, M.I.; Britten, C.J.
Measurement of alpha(1-3)fucosyltransferase activity using scintillation proximity
Anal. Biochem.
255
8-12
1998
Homo sapiens
Britten, C.J.; Bird, M.I.
Chemical modification of an alpha3-fucosyltransferase; definition of amino acid residues essential for enzyme activity
Biochim. Biophys. Acta
1334
57-64
1997
Homo sapiens
Hada, T.; Fukui, K.; Ohno, M.; Akamatsu, S.; Yazawa, S.; Enomoto, K.; Yamaguchi, K.; Matsuda, Y.; Amuro, Y.; et al.
Increased plasma alpha-(1->3)-L-fucosyltransferase activities in patients with hepatocellular carcinoma
Glycoconjugate J.
12
627-631
1995
Homo sapiens
Johnson, P.H.; Donald, A.S.; Clarke, J.L.; Watkins, W.M.
Purification, properties and possible gene assignment of an alpha 1,3-fucosyltransferase expressed in human liver
Glycoconjugate J.
12
879-893
1995
Homo sapiens
Robinson, N.E.; de Vries, T.; Davis, R.E.; Stults, C.L.M.; Watson, S.R.; van den Eijnden, D.H.; Macher, B.A.
Expression of fucosylated antigens and alpha1,3 fucosyltransferases in human leukemia cell lines
Glycobiology
4
317-326
1994
Homo sapiens
Holmes, E.H.; Xu, Z.; Sherwood, A.L.; Macher, B.A.
Structure-function analysis of human alpha1->3fucosyltransferases. A GDP-fucose-protected, N-ethylmaleimide-sensitive site in FucT-III and FucT-V corresponds to Ser178 in FucT-IV
J. Biol. Chem.
270
8145-8151
1995
Homo sapiens
Easton, E.W.; Schiphorst, W.E.; van Drunen, E.; van der Schoot, C.E.; van den Eijnden, D.H.
Human myeloid alpha 3-fucosyltransferase is involved in the expression of the sialyl-Lewis(x) determinant, a ligand for E- and P-selectin
Blood
81
2978-2986
1993
Homo sapiens
Candelier, J.J.; Mollicone, R.; Mennesson, B.; Bergemer, A.M.; Henry, S.; Coullin, P.; Oriol, R.
alpha-3-Fucosyltransferases and their glycoconjugate antigen products in the developing human kidney
Lab. Invest.
69
449-459
1993
Homo sapiens
Jezequel-Cuer, M.; N'Guyen-Cong, H.; Biou, D.; Durand, G.
Oligosaccharide specificity of normal human hepatocyte alpha1-3 fucosyltransferase
Biochim. Biophys. Acta
1157
252-258
1993
Homo sapiens
Weston, B.W.; Smith, P.L.; Kelly, R.J.; Lowe, J.B.
Molecular cloning of a fourth member of a human alpha(1,3) fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes
J. Biol. Chem.
267
24575-24584
1992
Homo sapiens (P51993), Homo sapiens
Galan, M.C.; Dodson, C.S.; Venot, A.P.; Boons, G.J.
Glycosyltransferase activity can be selectively modulated by chemical modifications of acceptor substrates
Bioorg. Med. Chem. Lett.
14
2205-2208
2004
Homo sapiens
Bryan, M.C.; Lee, L.V.; Wong, C.H.
High-throughput identification of fucosyltransferase inhibitors using carbohydrate microarrays
Bioorg. Med. Chem. Lett.
14
3185-3188
2004
Homo sapiens
Kawar, Z.S.; Haslam, S.M.; Morris, H.R.; Dell, A.; Cummings, R.D.
Novel poly-GalNAcbeta1-4GlcNAc (LacdiNAc) and fucosylated poly-LacdiNAc N-glycans from mammalian cells expressing beta1,4-N-acetylgalactosaminyltransferase and alpha1,3-fucosyltransferase
J. Biol. Chem.
280
12810-12819
2005
Homo sapiens
Miyashiro, M.; Furuya, S.; Sugita, T.
A high-throughput screening system for alpha1-3 fucosyltransferase-VII inhibitor utilizing scintillation proximity assay
Anal. Biochem.
338
168-170
2005
Homo sapiens
Miyashiro, M.; Furuya, S.; Sugita, T.
Development of a sensitive separation and quantification method for sialyl Lewis X and Lewis X involving anion-exchange chromatography: biochemical characterization of alpha1-3 fucosyltransferase-VII
J. Biochem.
136
723-731
2004
Homo sapiens
Satoh, T.; Kanai, Y.; Wu, M.; Yokozeki, H.; Kannagi, R.; Lowe, J.B.; Nishioka, K.
Synthesis of alpha(1,3) fucosyltransferases IV- and VII-dependent eosinophil selectin ligand and recruitment to the skin
Am. J. Pathol.
167
787-796
2005
Homo sapiens, Mus musculus (Q11127), Mus musculus (Q11131)
Azuma, Y.; Kurusu, Y.; Sato, H.; Higai, K.; Matsumoto, K.
Increased expression of Lewis X and Y antigens on the cell surface and FUT 4 mRNA during granzyme B-induced Jurkat cell apoptosis
Biol. Pharm. Bull.
30
655-660
2007
Homo sapiens
Salo, H.; Sievi, E.; Suntio, T.; Mecklin, M.; Mattila, P.; Renkonen, R.; Makarow, M.
Co-expression of two mammalian glycosyltransferases in the yeast cell wall allows synthesis of sLex
FEMS Yeast Res.
5
341-350
2005
Homo sapiens
Mnster, J.; Ziegelmller, P.; Spillner, E.; Bredehorst, R.
High level expression of monomeric and dimeric human alpha1,3-fucosyltransferase V
J. Biotechnol.
121
448-457
2006
Homo sapiens
Petit, D.; Maftah, A.; Julien, R.; Petit, J.M.
En bloc duplications, mutation rates, and densities of amino acid changes clarify the evolution of vertebrate alpha-1,3/4-fucosyltransferases
J. Mol. Evol.
63
353-364
2006
Ambystoma tigrinum (Q49ME5), Danio rerio (Q2VU44), Danio rerio (Q32WF4), Gallus gallus (Q8UVZ3), Homo sapiens (Q495W5), Takifugu rubripes (Q2KQ71), Takifugu rubripes (Q70AG8), Takifugu rubripes (Q70AG9), Takifugu rubripes (Q70AH0), Takifugu rubripes (Q70AH1), Takifugu rubripes (Q70AH2), Takifugu rubripes (Q70AH3), Takifugu rubripes (Q70AH4), Xenopus laevis (Q6WNG3), Xenopus tropicalis (Q49ME6)
Brito, C.; Gouveia, R.; Costa, J.
Stable expression of an active soluble recombinant form of human fucosyltransferase IX in Spodoptera frugiperda Sf9 cells
Biotechnol. Lett.
29
1623-1630
2007
Homo sapiens
Yang, X.; Zhang, Z.; Jia, S.; Liu, Y.; Wang, X.; Yan, Q.
Overexpression of fucosyltransferase IV in A431 cell line increases cell proliferation
Int. J. Biochem. Cell Biol.
39
1722-1730
2007
Homo sapiens (P22083)
Brito, C.; Escrevente, C.; Reis, C.A.; Lee, V.M.; Trojanowski, J.Q.; Costa, J.
Increased levels of fucosyltransferase IX and carbohydrate Lewis(x) adhesion determinant in human NT2N neurons
J. Neurosci. Res.
85
1260-1270
2007
Homo sapiens (Q5Q0U2), Homo sapiens
Ahsen, O.; Voigtmann, U.; Klotz, M.; Nifantiev, N.; Schottelius, A.; Ernst, A.; Mueller-Tiemann, B.; Parczyk, K.
A miniaturized high-throughput screening assay for fucosyltransferase VII
Anal. Biochem.
372
96-105
2008
Homo sapiens
Groux-Degroote, S.; Krzewinski-Recchi, M.A.; Cazet, A.; Vincent, A.; Lehoux, S.; Lafitte, J.J.; Van Seuningen, I.; Delannoy, P.
IL-6 and IL-8 increase the expression of glycosyltransferases and sulfotransferases involved in the biosynthesis of sialylated and/or sulfated Lewisx epitopes in the human bronchial mucosa
Biochem. J.
410
213-223
2008
Homo sapiens
Brito, C.; Kandzia, S.; Graca, T.; Conradt, H.S.; Costa, J.
Human fucosyltransferase IX: specificity towards N-linked glycoproteins and relevance of the cytoplasmic domain in intra-Golgi localization
Biochimie
90
1279-1290
2008
Homo sapiens (Q5Q0U2), Homo sapiens
Maeda, T.; Nishimura, S.
FRET-based direct and continuous monitoring of human fucosyltransferases activity: an efficient synthesis of versatile GDP-L-fucose derivatives from abundant D-galactose
Chemistry
14
478-487
2008
Homo sapiens
Wang, H.; Wang, Q.Y.; Zhang, Y.; Shen, Z.H.; Chen, H.L.
Alpha1,3 Fucosyltransferase-VII modifies the susceptibility of apoptosis induced by ultraviolet and retinoic acid in human hepatocarcinoma cells
Glycoconj. J.
24
207-220
2007
Homo sapiens
Lin, C.H.; Lin, C.W.; Khoo, K.H.
Proteomic identification of specific glycosyltransferases functionally implicated for the biosynthesis of a targeted glyco-epitope
Proteomics
8
475-483
2008
Homo sapiens
Stacke, C.; Ziegelmueller, P.; Hahn, U.
Comparison of expression systems for human fucosyltransferase IX
Eur. J. Cell Biol.
89
35-38
2010
Homo sapiens
Norden, R.; Nystroem, K.; Olofsson, S.
Activation of host antiviral RNA-sensing factors necessary for herpes simplex virus type 1-activated transcription of host cell fucosyltransferase genes FUT3, FUT5, and FUT6 and subsequent expression of sLe(x) in virus-infected cells
Glycobiology
19
776-788
2009
Homo sapiens
Wang, Q.Y.; Zhang, Y.; Shen, Z.H.; Chen, H.L.
alpha1,3 fucosyltransferase-VII up-regulates the mRNA of alpha5 integrin and its biological function
J. Cell. Biochem.
104
2078-2090
2008
Homo sapiens
Ponnampalam, A.P.; Rogers, P.A.
Expression and regulation of fucosyltransferase 4 in human endometrium
Reproduction
136
117-123
2008
Homo sapiens
Guo, Q.; Guo, B.; Wang, Y.; Wu, J.; Jiang, W.; Zhao, S.; Qiao, S.; Wu, Y.
Functional analysis of alpha1,3/4-fucosyltransferase VI in human hepatocellular carcinoma cells
Biochem. Biophys. Res. Commun.
417
311-317
2012
Homo sapiens
Seelhorst, K.; Stacke, C.; Ziegelmueller, P.; Hahn, U.
N-Glycosylations of human alpha1,3-fucosyltransferase IX are required for full enzyme activity
Glycobiology
23
559-567
2013
Homo sapiens
Li, W.; Zhang, W.; Luo, J.; Cao, A.; Zhang, Y.; Huang, D.; Sheng, W.; Cai, S.; Li, J.
Alpha1,3 Fucosyltransferase VII plays a role in colorectal carcinoma metastases by promoting the carbohydration of glycoprotein CD24
Oncol. Rep.
23
1609-1617
2010
Homo sapiens
Yang, X.; Liu, S.; Yan, Q.
Role of fucosyltransferase IV in epithelial-mesenchymal transition in breast cancer cells
Cell Death Dis.
4
e735
2013
Homo sapiens (P22083)
Seelhorst, K.; Pahnke, K.; Meier, C.; Hahn, U.
Tagging glycoproteins with fluorescently labeled GDP-fucoses by Using alpha1,3-fucosyltransferases
ChemBioChem
16
1919-1924
2015
Helicobacter pylori (O30511), Homo sapiens (Q11130), Homo sapiens (Q9Y231)
Li, D.; Sun, H.; Bai, G.; Wang, W.; Liu, M.; Bao, Z.; Li, J.; Liu, H.
alpha-1,3-Fucosyltransferase-VII siRNA inhibits the expression of SLex and hepatocarcinoma cell proliferation
Int. J. Mol. Med.
42
2700-2708
2018
Homo sapiens
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