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Information on EC 2.4.1.69 - type 1 galactoside alpha-(1,2)-fucosyltransferase
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EC Tree
2.4.1.69 type 1 galactoside alpha-(1,2)-fucosyltransferaseIUBMB Comments
The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 1 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 1 antigen. In humans the main enzyme performing this reaction is encoded by the FUT2 gene (also known as the Secretor gene), which is also able to act on type 2 substrates (see EC 2.4.1.344). The enzyme from the bacterium Helicobacter pylori cannot act on type 2 substrates.
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Word Map
- 2.4.1.69
-
fucosylation
- oligosaccharide
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sialylated
- glycans
- glycosyltransferases
- epitope
- lectin
-
sialyltransferase
- glycolipids
- selectins
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histo-blood
- glycoconjugates
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nonsecretors
-
e-selectin
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n-acetylglucosaminyltransferase
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fucts
- n-acetyllactosamine
- asialofetuin
- alpha-l-fucosidase
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bombay
- xyloglucan
-
lewisa
-
h-type
- 2'-fucosyllactose
- norovirus
-
fucosidase
- fuc-tvii
-
hyperacute
-
sialyl-lewis
-
difucosylated
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xenoantigens
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alpha1,3-galactosyltransferase
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xylosyltransferase
- psgl-1
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alpha1-6
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xenoreactive
- lactosamine
- gnt-iii
-
1-3glcnac
- medicine
-
hbgas
- alpha-gal
- neuac
- synthesis
- analysis
- tamarind
- lacto-n-biose
-
fucose-containing
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
a-(1->/2)-L-GalT, alpha (1,2)fucosyltransferase, alpha (1,2)fucosyltransferase 2, alpha (1,2)fucosyltransferase I, alpha 1, 2-fucosyltransferase 1, alpha(1,2)-fucosyltransferase, alpha(1,2)-fucosyltransferase-I, alpha(1,2)fucosyltransferase, alpha(1,2)fucosyltransferase I, alpha-(1,2)-fucosyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-(1->2)-L-fucosyltransferase
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-
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alpha-1,2-fucosyltransferase
alpha-2-fucosyltransferase
alpha-2-L-fucosyltransferase
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alpha-L-fucosyltransferase
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alpha1,2-fucosyltransferase
alpha1,2-FucT
alpha1,2FT
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-
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alpha1,2fucosyltransferase
alpha1-2FucT
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-
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alpha1->2-fucosyltransferase
alpha1->2-FucT
alpha2-fucosyltransferase
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dual function as beta3-galactosyltransferase/alpha2-fucosyltransferase
alpha2FT
beta-galactoside alpha1-2fucosyltransferase
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blood group H alpha-2-fucosyltransferase
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blood-group substance H-dependent fucosyltransferase
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CE2FT-2
EC 2.4.1.89
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formerly
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fucosyltransferase, guanosine diphosphofucose-galactoside 2-L-
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fucosyltransferase, guanosine diphosphofucose-glycoprotein 2-alpha-
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fucosyltransferase, guanosine diphosphofucose-lactose
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FucT
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FUT1
FUT2
futC
galactoside 2-alpha-L-fucosyltransferase
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GDP fucose-lactose fucosyltransferase
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GDP-beta-L-fucose:beta-D-galactosyl-R 2-alpha-L-fucosyltransferase
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GDP-fucose:GM1 alpha1-2fucosyltransferase
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GDP-L-fucose:beta-D-galactosyl-R-alpha-L-fucosyltransferase
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GDP-L-fucose:lactose fucosyltransferase
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GDPFuc:beta-D-galactoside alpha1,2-fucosyltransferase
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guanosine diphospho-L-fucose-lactose fucosyltransferase
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guanosine diphosphofucose-beta-D-galactosyl-alpha-2-L-fucosyltransferase
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guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide alpha-L-fucosyltransferase
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guanosine diphosphofucose-glycoprotein 2-alpha-L-fucosyltransferase
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H gene-encoded beta-galactoside alpha1->2 fucosyltransferase
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H-gene-encoded beta-galactoside alpha1-2fucosyltransferase
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Se gene-encoded beta-galactoside alpha1->2 fucosyltransferase
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Sec1
secretor-type beta-galactoside alpha1-2fucosyltransferase
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WbgL
WbiQ
WbsJ
wbwK
alpha-2-fucosyltransferase
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-
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CE2FT-2
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gene encoding an alpha1,2fucosyltransferase without activity towards Galbeta-O-p-nitrophenol or Galalpha-O-p-nitrophenol
WbsJ
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gene encoding an alpha1,2fucosyltransferase in Escherichia coli with a broad substrate specifity
WbsJ
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gene encoding an alpha1,2fucosyltransferase in Escherichia coli with a broad substrate specifity
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wbwK
Q5JBG3
gene encoding an alpha1,2fucosyltransferase in Escherichia coli which is only active with substrates containing the Galbeta1,3GalNAcalpha-structure (T-antigen) to form H-type 3 blood group antigen (Fucalpha1,2Galbeta1,3GalNAcalpha-OR) but not with Galbeta-OMe
wbwK
Q5JBG3
gene encoding an alpha1,2fucosyltransferase in Escherichia coli which is only active with substrates containing the Galbeta1,3GalNAcalpha-structure (T-antigen) to form H-type 3 blood group antigen (Fucalpha1,2Galbeta1,3GalNAcalpha-OR) but not with Galbeta-OMe
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R
-
-
-
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GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R
either a rapid equilibrium random kinetic mechanism or a steady state ordered mechanism with GDP-L-fucose binding first
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R alpha-(1,2)-L-fucosyltransferase (configuration-inverting)
The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 1 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 1 antigen. In humans the main enzyme performing this reaction is encoded by the FUT2 gene (also known as the Secretor gene), which is also able to act on type 2 substrates (see EC 2.4.1.344). The enzyme from the bacterium Helicobacter pylori cannot act on type 2 substrates.
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CAS REGISTRY NUMBER
COMMENTARY
56093-23-3
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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
GDP-beta-L-fucose + 2-nitrophenyl beta-D-galactopyranoside
GDP + 2-nitrophenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
-
-
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-galactosamine
residues of H type 3 epitopes, reaction of EC 2.4.1.69
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
residues of H type 2 epitopes
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine
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i.e. N-acetyllactosamine, reaction of EC 2.4.1.344
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-
?
GDP-beta-L-fucose + D-Gal-beta-(1,2)-D-Glc-beta-O-methyl
GDP + L-Fuc-alpha-(1,2)-D-Gal-beta-(1,2)-D-Glc-beta-O-methyl
-
-
-
-
?
GDP-beta-L-fucose + D-Gal-beta-(1,4)-D-Glc-beta-O-methyl
GDP + L-Fuc-alpha-(1,2)-D-Gal-beta-(1,4)-D-Glc-beta-O-methyl
-
-
-
-
?
GDP-beta-L-fucose + D-Gal-beta-(1,6)-D-Glc-beta-O-methyl
GDP + L-Fuc-alpha-(1,2)-D-Gal-beta-(1,6)-D-Glc-beta-O-methyl
-
-
-
-
?
GDP-beta-L-fucose + D-Gal-beta-(1->3)-D-Glcbeta-O-methyl
GDP + L-Fuc-alpha-(1->2)-D-Gal-beta-(1->3)-D-Glc-beta-O-methyl
-
-
-
-
?
GDP-beta-L-fucose + Gal(beta1-3)GlcNAc
?
28% activity compared to D-lactose
-
-
?
GDP-beta-L-fucose + Gal(beta1-4)GlcNAc
?
85% activity compared to D-lactose
-
-
?
GDP-beta-L-fucose + Galbeta(1-3)GalNAc
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAc
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-
-
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ir
GDP-beta-L-fucose + Galbeta(1-3)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAc
-
-
-
-
?
GDP-beta-L-fucose + Galbeta(1-3)GalNAcalpha-O-p-nitrophenol
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAcalpha-O-p-nitrophenol
-
-
-
-
ir
GDP-beta-L-fucose + Galbeta(1-3)GalNAcalpha-OMe
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAcalpha-OMe
GDP-beta-L-fucose + Galbeta(1-3)GalNAcalpha-R
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAcalpha-R
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-
-
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ir
GDP-beta-L-fucose + Galbeta(1-3)GlcNAcbeta-O-p-nitrophenol
GDP + Fucalpha(1-2)Galbeta(1-3)GlcNAcbeta-O-p-nitrophenol
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activity is low
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-
ir
GDP-beta-L-fucose + Galbeta(1-3)[Fucalpha(1-4)]GlcNAc
GDP + Fucalpha(1-2)Galbeta(1-3)[Fucalpha(1-4)]GlcNAc
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activity is low
-
-
ir
GDP-beta-L-fucose + Galbeta(1-3)[GlcNAcbeta(1-6)]GalNAcalpha-O-p-nitrophenol
GDP + Fucalpha(1-2)Galbeta(1-3)[GlcNAcbeta(1-6)]GalNAcalpha-O-p-nitrophenol
-
-
-
-
ir
GDP-beta-L-fucose + Galbeta-4-nitrophenyl
?
28% activity compared to D-lactose
-
-
?
GDP-beta-L-fucose + Galbeta-O-Me
GDP + L-Fucalpha(1-2)Galbeta-O-Me
-
-
-
-
?
GDP-beta-L-fucose + Galbeta-p-nitrophenol
GDP + L-Fucalpha(1-2)Galbeta-p-nitrophenol
-
-
-
-
?
GDP-beta-L-fucose + phenyl 2-acetamido-2-deoxy-3-O-beta-D-galactopyranosyl-alpha-D-galactopyranoside
GDP + phenyl L-fucosyl-alpha (1->2)-D-Gal-beta-(1->3)-alpha-D-GalNAc
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-
-
-
?
GDP-beta-L-fucose + phenyl beta-D-galactopyranoside
GDP + phenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
-
-
-
?
GDP-beta-L-fucose + phenyl beta-D-thiogalactopyranoside
GDP + phenyl L-fucosyl-alpha-(1->2)-beta-D-thiogalactopyranoside
-
-
-
-
?
GDP-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
Fucalpha1-2Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc + GDP
-
-
-
-
?
GDP-L-fucose + 6-sulfoGalbeta(1-4)GlcNAcbeta-O-methyl
GDP + L-Fucalpha(1-2)6-sulfoGalbeta(1-4)GlcNAcbeta-O-methyl
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-
-
-
?
GDP-L-fucose + agalacto-asialofetuin
GDP + alpha-L-fucosyl-1,2-agalacto-asialofetuin
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-
-
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?
GDP-L-fucose + arabinogalactan protein
?
-
isoforms FUT4.1 and FUT 6 incorporate terminal alpha-L-fucose residues on the C-2 positions of adjacent arabinose residues of arabinogalactan proteins
-
-
?
GDP-L-fucose + asialo alpha1 acid glycoprotein
GDP + alpha-L-fucosyl-1,2-asialo alpha1 acid glycoprotein
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-
-
-
?
GDP-L-fucose + beta-D-galactose-beta-O-2-(2-carbomethoxyethylthio)ethyl
?
-
-
-
-
?
GDP-L-fucose + beta-methyl-D-galactopyranoside
GDP + alpha-L-fucosyl-1,2-beta-methyl-D-galactopyranoside
-
-
-
-
?
GDP-L-fucose + D-Galbeta(1-2)D-Xylalpha(1-6)D-Glcbeta(1-4)D-Glc
GDP + L-Fucalpha(1-2)-D-Galbeta1-2-D-Xylalpha1-6-D-Glcbeta1-4-D-Glc
GDP-L-fucose + Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc-ceramide
GDP + L-Fucalpha(1-2)Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc-ceramide
-
-
-
?
GDP-L-fucose + GalalphaCH3
GDP + L-Fucalpha(1-2)GalalphaCH3
-
0.1% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-3)Ara
GDP + L-Fucalpha(1-2)Galbeta(1-3)Ara
-
3.3% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-3)GalNAcbeta(1-4)(NeuAcalpha(2-3))Galbeta(1-4)Glcbeta1-ceramide
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAcbeta(1-4)(NeuAcalpha(2-3))Galbeta(1-4)Glcbeta1-cera mide
-
-
-
?
GDP-L-fucose + Galbeta(1-3)GalNAcbeta1-OCH2CH=CH2
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAcbeta1-OCH2CH=CH2
-
-
-
-
?
GDP-L-fucose + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
-
84% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-3)GlcNAcbeta-O-allyl/acrylamide copolymer
GDP + ?
-
-
-
-
?
GDP-L-fucose + Galbeta(1-3)GlcNAcbeta-O-benzyl
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAcbeta-O-benzyl
-
-
-
-
?
GDP-L-fucose + Galbeta(1-4)Glc
GDP + L-Fucalpha(1-2)Galbeta(1-4)Glc
-
4.2% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-4)Glc-beta-O-2-(2-carbomethoxyethylthio)ethyl
GDP + L-Fucalpha(1-2)Galbeta(1-4)Glc-beta-O-2-(2-carbomethoxyethylthio)ethyl
-
-
-
-
?
GDP-L-fucose + Galbeta(1-4)GlcNAc
GDP + L-Fucalpha(1-2)Galbeta(1-4)GlcNAc
-
7.5% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-4)GlcNAc(1-3)Galbeta(1-4)Glc
GDP + L-Fucalpha(1-2)Galbeta(1-4)GlcNAc(1-3)Glabeta(1-4)Glc
-
2.8% of the activity with Galbeta(1-3)GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-4)GlcNAc-beta-O-2-(2-carbomethoxyethylthio)ethyl
GDP + L-Fucalpha(1-2)Galbeta(1-4)Glc-beta-O-2-(2-carbomethoxyethylthio)ethyl
-
-
-
-
?
GDP-L-fucose + Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc-ceramide
GDP + L-Fucalpha(1-2)Galbeta(1-4)GlcNAcbeta(1-3)Galbeta(1-4)Glc-ceramide
-
-
-
-
?
GDP-L-fucose + Galbeta(1-4)GlcNAcbeta-O-benzyl
GDP + L-Fucalpha(1-2)Galbeta(1-4)GlcNAcbeta-O-benzyl
-
-
-
-
?
GDP-L-fucose + Galbeta(1-4)Man
GDP + L-Fucalpha(1-2)Galbeta(1-4)Man
-
2.7% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OH
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OH
GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OMe
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OMe
GDP-L-fucose + GalbetaCH3
GDP + L-Fucalpha(1-2)GalbetaCH3
-
2.6% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + intestinal glycoprotein
GDP + alpha-L-fucosyl-1,2-intestinal glycoprotein
-
-
-
-
?
GDP-L-fucose + p-nitrophenyl beta-D-fucoside
GDP + alpha-L-fucosyl-1,2-nitrophenyl beta-D-fucoside
-
-
-
-
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
GDP-L-fucose + porcine submaxillary mucin
GDP + alpha-L-fucosyl-1,2-porcine submaxillary mucin
-
-
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
residues of H type 3 epitopes, reaction of EC 2.4.1.69
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
residues of H type 3 epitopes
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
residues of H type 1 epitopes, reaction of EC 2.4.1.69
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
residues of H type 1 epitopes
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
-
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
-
i.e. lacto-N-biose I
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
-
i.e. lacto-N-biose I, reaction of EC 2.4.1.69
82% of the activity with phenyl beta-D-galactopyranoside
-
?
GDP-beta-L-fucose + D-galactose
?
70% activity compared to D-lactose
-
-
?
GDP-beta-L-fucose + D-galactose
?
70% activity compared to D-lactose
-
-
?
GDP-beta-L-fucose + D-lactose
GDP + 2'-fucosyl-D-lactose
100% activity
-
-
?
GDP-beta-L-fucose + D-lactose
GDP + 2'-fucosyl-D-lactose
100% activity
-
-
?
GDP-beta-L-fucose + D-lactulose
GDP + 2'-fucosyl-D-lactulose
125% activity compared to D-lactose
-
-
?
GDP-beta-L-fucose + D-lactulose
GDP + 2'-fucosyl-D-lactulose
125% activity compared to D-lactose
-
-
?
GDP-beta-L-fucose + Gal-beta-OR
GDP + L-Fucalpha(1-2)Galbeta-OR
Q5JBG3
-
-
-
ir
GDP-beta-L-fucose + Gal-beta-OR
GDP + L-Fucalpha(1-2)Galbeta-OR
Q5JBG3
-
-
-
ir
GDP-beta-L-fucose + Galbeta(1-3)GalNAcalpha-OMe
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAcalpha-OMe
Q5JBG3
-
-
-
ir
GDP-beta-L-fucose + Galbeta(1-3)GalNAcalpha-OMe
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAcalpha-OMe
Q5JBG3
-
-
-
ir
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
fut1, fut2, and sec1 genes encode proteins that only can alpha1,2-fucosylate type 3/4, GM1 and galacto-N-biose acceptors
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the enzyme transfers fucose equally well to Galbeta(1-3)GlcNAc type and Galbeta(1-4)GlcNAc type substrates. Galbeta1-3GalNAc structures are less efficient acceptors
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
acceptor specificity, overview. C6-sulfation of terminal Gal in the LacNAc unit increases acceptor efficiency, C-6 sialylation abolishes acceptor ability, C6-sulfation of GlcNAc in LacNAc type 2 decreases by 80% the acceptor ability, whereas LacNAc type 1 is unaffected, the C-4 hydroxyl rather than the C-6 hydroxyl group of the GlcNAc moiety in LacNAc type 1 is essential for activity, the acrylamide copolymer of Galbeta(1-3)GlcNAcbeta-O-Al is the best acceptor among the acrylamide copolymers, Lewis x does not serve as an acceptor
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
detailed characterization of specificity
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the acid form of the enzyme is probably involved in glycoprotein synthesis in vivo
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
fucosyltransferase 1 may contribute to pathological prostatic growth
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
enzyme is involved in expression of blood group H, Lewis b from Lewis a and Globo H
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the galactoside 2-alpha-L-fucosyltransferase gene determines the expression of terminal L-Fucalpha(1-2)Galbeta epitopes
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
fucosyltransferase 1 may contribute to pathological prostatic growth
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the enzyme forms the Fuc(1-2)Gal linkage with oligosaccharides, glycoproteins, and glycolipids which contain nonreducing terminal galactose residues and shows no absolute specificity for a particular penultimate residue or for the linkage between the galactose and the penultimate residue. The enzyme fucosylates human Bombay" erythrocytes which lack cell surface Fucalpha1-2Gal structures
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the enzyme forms exclusively L-Fucalpha(1-2)Gal linkage with a variety of acceptor substrates
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + D-galactose
GDP + alpha-L-fucosyl-1,2-D-galactose
-
-
-
?
GDP-L-fucose + D-Galbeta(1-2)D-Xylalpha(1-6)D-Glcbeta(1-4)D-Glc
GDP + L-Fucalpha(1-2)-D-Galbeta1-2-D-Xylalpha1-6-D-Glcbeta1-4-D-Glc
-
-
-
?
GDP-L-fucose + D-Galbeta(1-2)D-Xylalpha(1-6)D-Glcbeta(1-4)D-Glc
GDP + L-Fucalpha(1-2)-D-Galbeta1-2-D-Xylalpha1-6-D-Glcbeta1-4-D-Glc
-
-
-
?
GDP-L-fucose + D-Galbeta(1-2)D-Xylalpha(1-6)D-Glcbeta(1-4)D-Glc
GDP + L-Fucalpha(1-2)-D-Galbeta1-2-D-Xylalpha1-6-D-Glcbeta1-4-D-Glc
-
-
-
?
GDP-L-fucose + D-Galbeta(1-2)D-Xylalpha(1-6)D-Glcbeta(1-4)D-Glc
GDP + L-Fucalpha(1-2)-D-Galbeta1-2-D-Xylalpha1-6-D-Glcbeta1-4-D-Glc
-
-
-
?
GDP-L-fucose + galacto-N-biose
GDP + alpha-L-fucosyl-1,2-galacto-N-biose
-
-
-
?
GDP-L-fucose + galacto-N-biose
GDP + alpha-L-fucosyl-1,2-galacto-N-biose
-
-
-
?
GDP-L-fucose + Galbeta(1-2)D-Xyl
GDP + L-Fucalpha(1-2)D-Galbeta(1-2)D-Xyl
-
-
-
?
GDP-L-fucose + Galbeta(1-2)D-Xyl
GDP + L-Fucalpha(1-2)D-Galbeta(1-2)D-Xyl
-
-
-
?
GDP-L-fucose + Galbeta(1-2)D-Xyl
GDP + L-Fucalpha(1-2)D-Galbeta(1-2)D-Xyl
-
-
-
?
GDP-L-fucose + Galbeta(1-2)D-Xyl
GDP + L-Fucalpha(1-2)D-Galbeta(1-2)D-Xyl
-
-
-
?
GDP-L-fucose + Galbeta(1-3)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAc
-
-
-
-
?
GDP-L-fucose + Galbeta(1-3)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAc
-
-
-
-
?
GDP-L-fucose + Galbeta(1-3)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAc
-
-
-
-
?
GDP-L-fucose + Galbeta(1-6)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-6)GalNAc
-
-
-
-
?
GDP-L-fucose + Galbeta(1-6)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-6)GalNAc
-
4.8% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OH
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OH
-
-
-
?
GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OH
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OH
-
-
-
?
GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OMe
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OMe
highest activity
-
-
?
GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OMe
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OMe
highest activity
-
-
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
-
-
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
-
-
-
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
i.e. Gal(1-3)GlcNAc
-
-
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
-
-
-
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
-
-
-
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
-
-
?
GDP-L-fucose + lacto-N-tetraose
GDP + lacto-N-fucopentaose I
-
-
-
?
GDP-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucosyl-1,2-N-acetyllactosamine
-
-
-
-
?
GDP-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucosyl-1,2-N-acetyllactosamine
-
-
-
-
?
GDP-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucosyl-1,2-N-acetyllactosamine
-
-
-
-
?
GDP-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucosyl-1,2-N-acetyllactosamine
-
-
-
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
-
-
-
-
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
-
-
-
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
-
-
-
-
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
-
-
-
-
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
-
-
-
-
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
-
-
-
?
additional information
?
-
-
dearabinosylated arabinogalactan proteins are not substrate acceptors for isoforms FUT4.1 and FUT6
-
-
-
additional information
?
-
the enzyme displays strict substrate specificity, displaying activity only towards acceptors that contain Gal-beta(1->3)-GalNAc-apha-OR linkages and does not recognize lactose, lactulose, Gal-alpha(1->3)-Gal-beta(1->4)Glc, alpha-GalGal-beta(1->4)-glucitol, and beta-D-Gal as acceptors
-
-
-
additional information
?
-
no activity with D-galactosamine, N-acetyl-D-galactosamine, Gal(beta1-4)Glcbeta1-Bn, Gal(beta1-4)Glcbeta1-octyl, Gal(beta1-4)[Fuc(alpha1-3)]Glc, Gal(beta1-4)GlcNAc(beta1-3)Gal(beta1-4)GlcNAcbeta-linker-tBoc, and Gal(alpha1-6)Glc(alpha1-2)Fru
-
-
-
additional information
?
-
no activity with D-galactosamine, N-acetyl-D-galactosamine, Gal(beta1-4)Glcbeta1-Bn, Gal(beta1-4)Glcbeta1-octyl, Gal(beta1-4)[Fuc(alpha1-3)]Glc, Gal(beta1-4)GlcNAc(beta1-3)Gal(beta1-4)GlcNAcbeta-linker-tBoc, and Gal(alpha1-6)Glc(alpha1-2)Fru
-
-
-
additional information
?
-
the enzyme displays strict substrate specificity, displaying activity only towards acceptors that contain Gal-beta(1->3)-GalNAc-apha-OR linkages and does not recognize lactose, lactulose, Gal-alpha(1->3)-Gal-beta(1->4)Glc, alpha-GalGal-beta(1->4)-glucitol, and beta-D-Gal as acceptors
-
-
-
additional information
?
-
-
secretor-type alpha1-2 fucosyltransferase shows significant lower affinity than the H-gene encoded enzyme for phenyl-beta-D-galactopyranoside and GDP-L-fucose as well as for type 1 oligosaccharide acceptors, Galbeta1-4GlcNAc. Type 1 acceptors, Galbeta1-3GlcNAc, and type 3 acceptors, Galbeta1-3GalNAc, are preferentially used by the secretor-type enzyme as compared with the H enzyme
-
-
-
additional information
?
-
-
enzyme favors certain glycoproteins containing polylactosamine units
-
-
-
additional information
?
-
-
alpha-galactosidase and alpha-1,2-fucosyltransferase can inhibit the expression of Gal-alpha-1,3-Gal synergistically, leading to stronger resistance of xenograft against cytolysis mediated by natural antibodies and complements
-
-
-
additional information
?
-
-
FUT1 is able to efficiently alpha(1,2)-fucosylate the O-linked glycans of PSGL-1 but not the sLex structures that bind too the P-selectin
-
-
-
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 20–30fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
-
additional information
?
-
-
the enzyme reduces terminal alpha(2,3)-sialylation in transfected cells and transgenic animals
-
-
-
additional information
?
-
-
FUT2 directs alpha2-fucosylation on type 1 chains on both N- and O-linked glycan structures
-
-
-
additional information
?
-
-
FUT2 regulates the expression of a carbohydrate on the gastrointestinal epitheliumstrong association is observed between the nonsense mutation 428G--A in the FUT2 gene and a slow disease progression of HIV-1 infection
-
-
-
additional information
?
-
-
FutC substrates are generated by both FutA and FutB, and their heptad repeat number correlates to Lewis y O-antigen polymer sizes
-
-
-
additional information
?
-
-
human secretor FUT2 gene, which codes for an alph(1,2)-fucosyltransferase synthesizing the H-type 1 antigen in saliva and mucosa, is associated with susceptibility to norovirus infections. the FUT2 nonsecretor (se428se428) genotype is associated with resistance to nosocomial and sporadic outbreaks with norovirus
-
-
-
additional information
?
-
-
enzyme accepts both precursors of type 1 and type 2 H epitopes, catalyzing reactions of EC 2.4.1.69 and EC 2.4.1.344. The enzyme does not display alpha-(1,3)-fucosyltransferase activity or alpha-(1, 4)-fucosyl transferase activity
-
-
-
additional information
?
-
-
the enzyme transfers fucose equally well to type I (Galbeta-(1->3)-GIcNAc) and type 2 (Galbeta-(1->4)-GIcNAc) substrates, reaction of EC 2.4.1.344, but type 3 (Galbeta-(1->3)-GalNAc) structures are less efficient acceptors
-
-
-
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 20–30fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
-
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 20–30fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
-
additional information
?
-
the enzyme shows a strong preference for terminal Galbeta1, 3GalNAc structures
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
residues of H type 3 epitopes, reaction of EC 2.4.1.69
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-galactosamine
residues of H type 3 epitopes, reaction of EC 2.4.1.69
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
residues of H type 1 epitopes, reaction of EC 2.4.1.69
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
residues of H type 2 epitopes
-
-
?
GDP-beta-L-fucose + phenyl beta-D-galactopyranoside
GDP + phenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
-
-
-
?
GDP-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
Fucalpha1-2Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc + GDP
-
-
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the acid form of the enzyme is probably involved in glycoprotein synthesis in vivo
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
fucosyltransferase 1 may contribute to pathological prostatic growth
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
enzyme is involved in expression of blood group H, Lewis b from Lewis a and Globo H
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the galactoside 2-alpha-L-fucosyltransferase gene determines the expression of terminal L-Fucalpha(1-2)Galbeta epitopes
-
-
-
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
fucosyltransferase 1 may contribute to pathological prostatic growth
-
-
-
additional information
?
-
-
alpha-galactosidase and alpha-1,2-fucosyltransferase can inhibit the expression of Gal-alpha-1,3-Gal synergistically, leading to stronger resistance of xenograft against cytolysis mediated by natural antibodies and complements
-
-
-
additional information
?
-
-
FUT1 is able to efficiently alpha(1,2)-fucosylate the O-linked glycans of PSGL-1 but not the sLex structures that bind too the P-selectin
-
-
-
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 20–30fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
-
additional information
?
-
-
FUT2 directs alpha2-fucosylation on type 1 chains on both N- and O-linked glycan structures
-
-
-
additional information
?
-
-
FUT2 regulates the expression of a carbohydrate on the gastrointestinal epitheliumstrong association is observed between the nonsense mutation 428G--A in the FUT2 gene and a slow disease progression of HIV-1 infection
-
-
-
additional information
?
-
-
FutC substrates are generated by both FutA and FutB, and their heptad repeat number correlates to Lewis y O-antigen polymer sizes
-
-
-
additional information
?
-
-
human secretor FUT2 gene, which codes for an alph(1,2)-fucosyltransferase synthesizing the H-type 1 antigen in saliva and mucosa, is associated with susceptibility to norovirus infections. the FUT2 nonsecretor (se428se428) genotype is associated with resistance to nosocomial and sporadic outbreaks with norovirus
-
-
-
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 20–30fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
-
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 20–30fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
10 mM, 6% of the activity with Mn2+; 10 mM, enzyme from gastric mucosa: 6.3% of the activation with Mn2+, enzyme from plasma: 108% of the activation with Mn2+
Ca2+
Co2+
Mg2+
Mn2+
additional information
Ca2+
-
10 mM, 45% of the activity with Mn2+; 10 mM, enzyme from gastric mucosa: 44.8% of the activation with Mn2+, enzyme from plasma: 94.2% of the activation with Mn2+
Ca2+
-
soluble and membrane-bound enzyme are active in absence of added cations, but addition of 10 mM Mn2+, Mg2+ or Ca2+ stimulates
Ca2+
-
the enzyme is active in absence of divalent metal ions, but is stimulated by Mn2+, Mg2+, Ca2+ or Co2+
Co2+
-
10 mM, 48% of the activity with Mn2+; 10 mM, enzyme from gastric mucosa: 48.6% of the activation with Mn2+, enzyme from plasma: 94.3% of the activation with Mn2+
Co2+
-
the enzyme is active in absence of divalent metal ions, but is stimulated by Mn2+, Mg2+, Ca2+ or Co2+
Mg2+
-
10 mM, 65% of the activity with Mn2+; 10 mM, enzyme from gastric mucosa: 65.3% of the activation with Mn2+, enzyme from plasma: 98.2% of the activation with Mn2+
Mg2+
-
soluble and membrane-bound enzyme are active in absence of added cations, but addition of 10 mM Mn2+, Mg2+ or Ca2+ stimulates
Mg2+
-
the enzyme is active in absence of divalent metal ions, but is stimulated by Mn2+, Mg2+, Ca2+ or Co2+
Mn2+
-
10 mM, best activator; divalent cation is essential for enzyme from gastric mucosa, maximal activity with 10 mM Mn2+. Enzyme from plasma is maximally activated with 10 mM Mn2+, but activity is also observed without the cation
Mn2+
-
soluble and membrane-bound enzyme are active in absence of added cations, but addition of 10 mM Mn2+, Mg2+ or Ca2+ stimulates
Mn2+
-
the enzyme is active in absence of divalent metal ions, but is stimulated by Mn2+, Mg2+, Ca2+ or Co2+
additional information
-
activity is found to be independent of divalent metal ions
additional information
the enzyme does not require the presence of a divalent metal to be enzymatically active
additional information
the enzyme shows no strict requirement for divalent metal ions
additional information
-
divalent cation is absolutely required, no activation with Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
-
i.e. lacto-N-neotetraose, competitive with respect to lacto-N-biose I
2-mercaptoethanol
-
complete inhibition of activity with lacto-N-biose I
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CHAPSO
-
the truncated enzyme is optimally activated by CHAPSO, showing little activity in absence
Triton CF-54
-
the native and the recombinant full-length enzyme display significant activity in absence of detergent or phospholipid and are optimally activated in presence of Triton CF-54 detergent
additional information
the enzyme exhibits full activity when 10 mM EDTA is present
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc-beta-O-PA8
-
H-gene encoded enzyme
2.5
Galbeta(1-4)GlcNAc-beta-O-2-(2-carbomethoxyethylthio)ethyl
-
H-endoced and Se-encoded enzyme
additional information
additional information
-
KM-value for asialofetuin: 3.33 mg/ml
-
3.2
beta-D-galactose-beta-O-2-(2-carbomethoxyethylthio)ethyl
-
H-gene encoded enzyme
8.5
beta-D-galactose-beta-O-2-(2-carbomethoxyethylthio)ethyl
-
Se-gene encoded enzyme
0.95
beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
-
pH 7.2, temperature not specified in the publication
0.0011
GDP-L-fucose
-
reaction with porcine submaxillary mucin or intestinal glycoprotein
0.079
GDP-L-fucose
-
reaction with phenyl-beta-D-galactoside, recombinant enzyme
0.3984
GDP-L-fucose
-
Km above 0.3984 mM, isoform FUT1 mutant C35T, in 50 mM Tris-HCl (pH 7.2), at 37°C; wild type isoform FUT1, in 50 mM Tris-HCl (pH 7.2), at 37°C
83.6
phenyl-beta-D-galactoside
-
wild type isoform FUT1, in 50 mM Tris-HCl (pH 7.2), at 37°C
125
phenyl-beta-D-galactoside
-
isoform FUT1 mutant C35T, in 50 mM Tris-HCl (pH 7.2), at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
GDP-L-fucose
-
wild type isoform FUT1, in 50 mM Tris-HCl (pH 7.2), at 37°C
0.011
phenyl-beta-D-galactoside
-
isoform FUT1 mutant C35T, in 50 mM Tris-HCl (pH 7.2), at 37°C; wild type isoform FUT1, in 50 mM Tris-HCl (pH 7.2), at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0183
GDP-L-fucose
-
wild type isoform FUT1, in 50 mM Tris-HCl (pH 7.2), at 37°C
0.000088
phenyl-beta-D-galactoside
-
isoform FUT1 mutant C35T, in 50 mM Tris-HCl (pH 7.2), at 37°C
0.000132
phenyl-beta-D-galactoside
-
wild type isoform FUT1, in 50 mM Tris-HCl (pH 7.2), at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.6
Galbeta(1,3)GalNAcalpha-O-allyl
-
reaction with 6-sulfoGalbeta(1,3)GlcNAcbeta-O-allyl
5.9
Galbeta(1,4)GlcNAcbeta(1,6)Galbeta(1,3)-GalNAcalpha-O-benzyl
-
reaction with 6-sulfoGalbeta(1,4)GlcNAcbeta-O-methyl
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.852
Q5JBG3
activity of WbwK-GST fusion protein with Galbeta(1-3)GalNAcalpha-O-benzyl as substrate; activity of WbwK-GST fusion protein with Galbeta1,3GalNAcalpha-O-benzyl as substrate
0.873
Q5JBG3
activity of WbwK-GST fusion protein with Galbeta(1-3)GalNAcalpha-O-methyl as substrate; activity of WbwK-GST fusion protein with Galbeta1,3GalNAcalpha-O-methyl as substrate
additional information
additional information
-
relative activity: lactose: 100%, Galbeta(1,4)Glcbeta-N3 (LacN3): 137%, Galbeta(1,4)Glcbeta-O-phenyl: 84.7%, Galbeta(1,4)Glcbeta-S-phenyl: 207%, Galbeta(1,4Glc)beta-1-NAc: 199%, Galbeta-p-nitrophenol: 30.4%, galactose: 35.7%, Galbeta-O-Me: 68.8%, Galbeta(1,4)GlcNAc: 12.4%, Galbeta(1,4)Fru: 380%, Galbeta(1,4)Man: 162%, Galbeta(1,3)GalNAcalpha-O-benzyl: 202%, Galbeta(1,3)GalNAcalpha-O-Me: 215%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.6
-
pH 6.0: 15% of maximal activity, pH 6.4: 59.2% of maximal activity, pH 6.8: 84.8% of maximal activity, pH 7.2-7.6: maximal activity, recombinant enzyme
6.5 - 7.8
-
pH 6.5: about 70% of maximal activity, pH 7.8: about 65% of maximal activity, enzyme from bone marrow
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16 - 30
-
16°C: 61% of maximal activity, 30°C: 62% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
349720, 489345, 489348, 489349, 489350, 489351, 489352, 489359, 489360, 489361, 489363, 489365, 657489, 657509, 659133, 680997, 681671, 682528, 690350, 690434, 692656, 693324, 703927, 723789, 740330, 740517
-
-
brenda
FUT2 gene polymorphisms in a Korean population. The se357/385 is a common secretor enzyme-deficient allele in the Korean population, and the se428, which is a common null allele in Africans and Caucasians, is quite rare
-
-
brenda
two fucosyltransferase 2 gene missense polymorphisms, G247S and F280S, are partly responsible for non-secretor status in a Caucasian population from Northern Portugal
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
gut colonization by symbiotic bacteria stimulates ERK and JNK signal transduction pathways, resulting in activation of transcription factors ATF2 and c-Jun, respectively. This increases transcription of fut2 mRNA and expression of alpha1,2/3-fucosyltransferase activity, resulting in a highly fucosylated intestinal mucosa characteristic of the adult mammalian gut. Blocking the ERK and JNK signaling cascade inhibits the ability of colonization to induce elevated fut2 mRNA and fucosyltransferase activity in the mature colon
brenda
-
down regulation of alpha1,2-fucosyltransferase activity is associated with human gastric tumorigenesis
brenda
-
e.g. hepatoma H35 cells, the enzyme is induced during early stages of chemical hepatocarcinogenesis in parenchymal cells of Fischer 344 rats fed a diet supplemented with 0.03% N-2-acetylaminofluorene, undetectable in normal liver tissue
brenda
-
an enhanced expression of CD173/CD174 and transcription of FUT1 is observed after treatment of human bone marrow endothelial cells (HBMEC) with tumor necrosis factor-alpha (TNF-alpha) or conditioned supernatants of the leukemia cell line KG1a
brenda
-
undifferentiated leukemic cells, K562, that have erythroid characteristics
brenda
-
prostatic epithelial cells derived from patients with benign prostatic hyperplasia and from patients with prostatic cancer
brenda
additional information
-
no cDNA detected in urinary bladder, the testis, the seminal vesicle, the ovary, the uterus, the spleen, the brain or muscle; no cDNA detected in urinary bladder, the testis, the seminal vesicle, the ovary, the uterus, the spleen, the brain or muscle
brenda
-
of donors of all ABO blood-groups examined, except those of the rare Oh (Bombay) and Bh phenotypes
brenda
-
only when the glands are from individuals who are secretors of the ABH blood-group substances
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
in roots, isoforms FUT4 and FUT6 genes are responsible for arabinogalactan fucosylation
physiological function
malfunction
-
absence of pgtA, wild-type O2 dependence of culmination
malfunction
-
the spontaneous G428A nonsense mutation in FUT2 provides strong but not absolute protection against symptomatic GII.4 Norovirus infection
malfunction
-
blocking enzyme expression in arthritis synovial fibroblasts reduces endothelial cell tube formation
physiological function
-
isoform Fta allows synthesis of H type 2 and H type 3 histo-blood group antigen epitopes at the cell surface. In Chinese hamster ovary cells transfected by FTA, FTA is able to synthesize H type 2 epitopes on a large set of glycoproteins; isoform Fta allows synthesis of H type 2 and H type 3 histo-blood group antigen epitopes at the cell surface. In Chinese hamster ovary cells transfected by FTA, FTA is able to synthesize H type 2 epitopes on a large set of glycoproteins
physiological function
Q5JBG3
Some Escherichia coli strains display human blood group antigens, so called O-antigen structures, on their cell surface to evade the immune system of the human host. alpha1,2fucosyltransferase are involved in the biosynthesis of O-antigen structures.; Some Escherichia coli strains display human blood group antigens, so called O-antigen structures, on their cell surface to evade the immune system of the human host. alpha1,2fucosyltransferase are involved in the biosynthesis of O-antigen structures.
physiological function
-
synthesis of human H-type 3 blood group structure in pharyngeal cells to secrete glycoconjugates to the nematode surface
physiological function
-
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.; Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
-
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
physiological function
-
Women homozygous for the rs492602 G allele had higher B12 levels. This allele is in strong linkage disequilibrium with the FUT2 W143X nonsecretor variant, suggesting a plausible mechanism for altered B12 absorption and plasma levels.
physiological function
-
the H antigen of human blood group is synthesized by alpha-(1,2)-fucosyltransferase
physiological function
-
the enzyme is responsible for synthesis of the H blood group and Lewis y antigens
physiological function
-
the upregulated expression of the enzyme is associated with advanced pathological stages and involved in cell proliferation, migration and invasion in ovarian cancer
physiological function
-
the enzyme is involved in the development of multidrug resistance of chronic myeloid leukemia cells and regulates the activity of EGFR/MAPK signaling pathway and the expression of P-glycoprotein
physiological function
-
Some Escherichia coli strains display human blood group antigens, so called O-antigen structures, on their cell surface to evade the immune system of the human host. alpha1,2fucosyltransferase are involved in the biosynthesis of O-antigen structures.; Some Escherichia coli strains display human blood group antigens, so called O-antigen structures, on their cell surface to evade the immune system of the human host. alpha1,2fucosyltransferase are involved in the biosynthesis of O-antigen structures.
-
Show AA Sequence and Transmembrane Helices (156 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
x * 50000, enzyme from serum, SDS-PAGE under reducing conditions
55000
59000
60000
61000
70000
x * 70000, recombinant, His- and pro-protein-tagged enzyme, SDS-PAGE
59000
-
x * 59000, His-tagged isoform FUT6, calculated from amino acid sequence
61000
-
x * 61000, His-tagged isoform FUT4.1, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
-
1 * 55000 under reducing and non-reducing conditions, 1 * 57000 under reducing conditions, SDS-PAGE
additional information
-
two enzyme species of 55000 Da and 60000 Da detected by SDS-PAGE
?
-
x * 59000, His-tagged isoform FUT6, calculated from amino acid sequence; x * 60000, His-tagged isoforms FUt4.1 and FUT6, SDS-PAGE; x * 61000, His-tagged isoform FUT4.1, calculated from amino acid sequence
?
x * 59000, calculated from amino acid sequence; x * 70000, recombinant, His- and pro-protein-tagged enzyme, SDS-PAGE
?
-
x * 59000, calculated from amino acid sequence; x * 70000, recombinant, His- and pro-protein-tagged enzyme, SDS-PAGE
-
homodimer
2 * 60000, GST-tagged enzyme, SDS-PAGE; 2 * 61000, calculated from amino acid sequence
homodimer
-
2 * 60000, GST-tagged enzyme, SDS-PAGE; 2 * 61000, calculated from amino acid sequence
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H152A
-
Km increased compared to wild-type using substrate lactulose and substrate GDP-fucose
H152R
-
Km increased compared to wild-type using substrate lactulose and substrate GDP-fucose
R154K
-
Km increased compared to wild-type using substrate lactulose and substrate GDP-fucose
R155A
-
Km increased compared to wild-type using substrate lactulose and substrate GDP-fucose
R155K
-
Km increased compared to wild-type using substrate lactulose and substrate GDP-fucose
C35T
-
the mutation is a polymorphism in the Chinese population and does not affect its mRNA transcription, but can slightly decrease the activity of human alpha-(1,2)-fucosyltransferase in vitro
F280S
-
missense polymorphism, almost inactive enzyme, responsible for some non-secretor cases
G247S
-
missense polymorphism, almost inactive enzyme, responsible for some non-secretor case
I129F
-
most frequent nonsense mutation of FUT2 in populations of Asian ancestry
S12F
-
the mutation does not significantly decrease the activity of alpha-(1,2)-fucosyltransferase and affect its kinetic property
W143X
-
Nonsense mutation of FUT2 with a allele frequency of 0.46 in populations of European ancestry. Individuals homozygous for the FUT2 nonsecretor genotype appear to be resistant to infection with Norovirus, suggesting that individuals homozygous for nonsecretor status may be unable to mediate host-microbe interactions.
additional information
additional information
-
fusion protein with a C-terminal HPC4-epitope tag is created
additional information
-
pgtA-null cells, developmental arrest in mild hypoxia
additional information
Q5JBG3
To demonstrate that the variable regions determine substrate specificity and to investigate which of the variable regions of R1,2-FucT is responsible, six chimeric R1,2-FucTs are constructed by domain swapping between Escherichia coli FucTs WbsJ and WbwK. Three chimeras are inactive, the other three chimeras have greater substrate spectra than FucT WbwK but lower activity than WbsJ.; To demonstrate that the variable regions determine substrate specificity and to investigate which of the variable regions of R1,2-FucT is responsible, six chimeric R1,2-FucTs are constructed by domain swapping between Escherichia coli FucTs WbsJ and WbwK. Three chimeras are inactive, the other three chimeras have greater substrate spectra than FucT WbwK but lower activity than WbsJ.
additional information
-
To demonstrate that the variable regions determine substrate specificity and to investigate which of the variable regions of R1,2-FucT is responsible, six chimeric R1,2-FucTs are constructed by domain swapping between Escherichia coli FucTs WbsJ and WbwK. Three chimeras are inactive, the other three chimeras have greater substrate spectra than FucT WbwK but lower activity than WbsJ.; To demonstrate that the variable regions determine substrate specificity and to investigate which of the variable regions of R1,2-FucT is responsible, six chimeric R1,2-FucTs are constructed by domain swapping between Escherichia coli FucTs WbsJ and WbwK. Three chimeras are inactive, the other three chimeras have greater substrate spectra than FucT WbwK but lower activity than WbsJ.
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additional information
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human bone marrow endothelial cells (HBMEC) FUT1-siRNA-transfectants display impaired in vitro angiogenesis when cultivated on extracellular matrix and in spheroid assays
additional information
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bp428 G>A is a spontaneous nonsense mutation, 739G > A substitution does not inactivate the enzyme
additional information
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the spontaneous G428A nonsense mutation in FUT2 provides not absolute protection against symptomatic GII.4 Norovirus infection: during a norovirus outbreak in an elderly nursing home only 1 of 17 nonsecretors was infected, whereas 70% of the secretors were infected
additional information
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recombinant full length enzyme has a specific activity over 80fold higher than the truncated enzyme missing the first 27 amino acid residues from the N-terminus, comprising the cytoplasmic and transmembrane domains. The native and the recombinant full-length enzyme display significant activity in absence of detergent or phospholipid and are optimally activated in presence of Triton CF-54 detergent. The truncated enzyme is optimally activated by CHAPSO, showing littel activity in absence
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27
at 27°C in 50 mM Tris-HCl buffer pH 7.6, the enzyme shows a half -life of 57 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography and Superdex 200 gel filtration
GST-WbsJ fusion protein is purified to homogeneity via GST affinity chromatography followed by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of gene FTB and FTC; transfection of Chinese hamster ovary cells; transfection of Chinese hamster ovary cells
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expressed as full-length protein with and without a C-terminal HPC4-epitope tag in human 293T cells
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expressed as GST fusion protein in Escherichia coli BL21 (DE3); expressed as GST fusion protein in Escherichia coli BL21 (DE3)
Q5JBG3
full length enzyme and truncated enzyme missing the first 27 amino acid residues from the N-terminus, comprising the cytoplasmic and transmembrane domains
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porcine endothelial cell line transfected with human alpha(1,2)-fucosyltransferase cDNA
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subcloned in COS-7 or CHOP cells (Chinese hamster ovary cells transformed with Polyoma large T antigen)
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the GST-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells
the transcription start site of FUT1 changes during differentiation of the erythroid lineage. The tissue-specific and stage-specific expression of the FUT1 are regulated by three distinct promoters. The 5'-flanking region of exon 2 consists of repetitive sequences. The start site of exon 2 is within the long terminal repeat. The repetitive sequences may play a role in the expression of the FUT1
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the wbsJ gene is overexpressed in Escherichia coli BL21 as a fusion protein with glutathione S-transferase (GST) at its N-terminus
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transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 20–30fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
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transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 20–30fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids; transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 20–30fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Fut4 mRNA expression is increased following coculture of epithelial cells with macrophages for 24 h (1.3fold) or 48 h (1.2fold)
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the enzyme expression is increased in ovarian cancer. Transient overexpression of c-Jun promotes the enzyme expression 3.86 -11.4fold
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
determination of GDP-L-fucose:galactoside 2'-fucosyltransferase in human serum employing o-nitrophenyl-beta-D-galactopyranoside, phenyl-2-acetamido-2-deoxy-3-O-beta-D-galactopyranosyl-alpha-D-galactopyranoside, or phenyl beta-D-thiogalactopyranoside as acceptors. The method can simultaneously monitor possible competing reactions which may interfere with determination of alpha-2-L-fucosyltransferase activity
medicine
synthesis
medicine
-
alpha-galactosidase and alpha-1,2-fucosyltransferase can inhibit the expression of Gal-alpha-1,3-Gal synergistically, leading to stronger resistance of xenograft against cytolysis mediated by natural antibodies and complements. It implies a practical significance of combined transgenic strategy with alpha galactosidase and alpha-1,2-fucosyltransferase
medicine
-
FUT1 can efficiently prevent the synthesis of slex antigens in hepatocarcinoma and colon carcinoma cells and their interaction with activated endothelia. The FUT-EGFP gene transfer approach would be expected to decrease or even suppress the initial vascular arrest of tumor cells and may provide a basis for the development of antimetastatic gene therapy
medicine
-
it is shown that human alpha(1,2)-fucosyltransferase activity is remarkably decreased (40-90%) in human gastric cancer and may serve as a potential tumor marker; tumor marker for human gastric cancer, down regulation of alpha1,2-fucosyltransferase activity is associated with human gastric tumorigenesis
medicine
-
sequence variations in the proximal promoter region of FUT2 in several human populations is studied. In African populations, two SNPs (17606C>T and 17721T>G) with intermediate frequency that affected the promoter activity in vitro with a cell type-specific pattern are found
medicine
-
using nude mice subcutaneously xenotransplanted with parental or FUT1-transduced hepatocarcinoma cells HepG2 it is shown that FUT1 displays a strong antitumorigenicity due to a defect in tumor vascularization
medicine
-
involvement of alpha 1-2-fucosyltransferase I (FUT1) and surface-expressed Lewis(y) (CD174) in first endothelial cell-cell contacts during angiogenesis is shown
medicine
-
systematic sequence analysis of the human FUT2 gene in healthy chinese and caucasian subjects identifies 18 sequence variations in the FUT2 gene, and 6 are novel
medicine
-
co-expression of the enzyme with 1,3-galactosyltransferase leads to a considerable reduction of the alpha-Gal antigen level on the surface of cells and a decrease of xenotransplant immunogenicity
synthesis
-
large-scale synthesis of H-antigen oligosaccharides by expressing Helicobacter pylori alpha1,2-fucosyltransferase in metabolically engineered Escherichia coli cells
synthesis
-
fast and efficient synthesis of a novel homologous series of L-fucosylated trisaccharides using the alpha-(1->2)-L-galactosyltransferase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scudder, P.R.; Chantler, E.N.
Glycosyltransferases of the human cervical epithelium. I. Characterization of a beta-galactoside alpha-2-L-fucosyltransferase and the identification of a beta-N-acetylglucosaminide alpha-3-L-fucosyltransferase
Biochim. Biophys. Acta
660
128-135
1981
Homo sapiens
brenda
Beyer, T.A.; Sadler, J.E.; Hill, R.L.
Purification to homogeneity of H blood group beta-galactoside alpha 1->2 fucosyltransferase from porcine submaxillary gland
J. Biol. Chem.
255
5364-5372
1980
Sus scrofa
brenda
Beyer, T.A.; Hill, R.L.
Enzymatic properties of the beta-galactoside alpha 1->2 fucosyltransferase from porcine submaxillary gland
J. Biol. Chem.
255
5373-5379
1980
Sus scrofa
brenda
Barreaud, J.P.; Saunier, K.; Souchaire, J.; Delourme, D.; Oulmouden, A.; Oriol, R.; Leveziel, H.; Julien, R.; Petit, J.M.
Three bovine alpha2-fucosyltransferase genes encode enzymes that preferentially transfer fucose on Galbeta1-3GalNAc acceptor substrates
Glycobiology
10
611-621
2000
Bos taurus, Bos taurus (Q28113)
brenda
Kyprianou, P.; Betteridge, A.; Donald, A.S.R.; Watkins, W.M.
Purification of the blood group H gene associated alpha-2-L-fucosyltransferase from human plasma
Glycoconjugate J.
7
573-588
1990
Homo sapiens
brenda
Basu, S.; Basu, M.; Chien, J.L.
Enzymatic synthesis of a blood group H-related glycosphingolipid by an alpha-fucosyltransferase from bovine spleen
J. Biol. Chem.
250
2956-2962
1975
Bos taurus
brenda
Grollman, A.P.
GDP-L-fucose:lactose fucosyltransferase from mammary gland
Methods Enzymol.
8
351-353
1966
Canis lupus familiaris
-
brenda
Chester, M.A.; Yates, A.D.; Watkins, W.M.
Phenyl beta-D-galactosylpyranoside as an acceptor substrate for the blood-group H gene-associated guanosine diphosphate L-fucose:beta-D-galactosyl alpha-2-L-fucosyltransferase
Eur. J. Biochem.
69
583-592
1976
Homo sapiens
-
brenda
Sarnesto, A.; Koehlin, T.; Thurin, J.; Blaszczyk-Thurin, M.
Purification of Hgene-encoded beta-galactoside alpha 1->2 fucosyltransferase from human serum
J. Biol. Chem.
265
15067-15075
1990
Homo sapiens
brenda
Sarnesto, A.; Koehlin, T.; Hindsgaul, O.; Thurin, J.; Blaszczyk-Thurin, M.
Purification of the secretor-type beta-galactoside alpha 1->2-fucosyltransferase from human serum
J. Biol. Chem.
267
2737-2744
1992
Homo sapiens
brenda
Pacuszka, T.; Koscielak, J.
alpha 1->2 Fucosyltransferase of human bone marrow
FEBS Lett.
41
348-351
1974
Homo sapiens
brenda
Chou, T.H.; Murphy, C.; Kessel, D.
Selective inhibition of a plasma fucosyltransferase by N-ethylmaleimide
Biochem. Biophys. Res. Commun.
74
1001-1006
1977
Homo sapiens
brenda
Bella, A.; Kim, Y.S.
Biosynthesis of intestinal glycoprotein: a study of an (1 lead to 2) fucosyltransferase in rat small intestinal mucosa
Arch. Biochem. Biophys.
147
753-761
1971
Rattus norvegicus
brenda
Bella, A.; Kim, Y.S.
Inhibition of rat small-intestinal alpha-(1-> 2)-fucosyltransferase
Biochem. J.
125
1157-1158
1971
Rattus norvegicus
brenda
Thurin, J.; Blaszczyk-Thurin, M.
Porcine submaxillary gland GDP-L-fucose: beta-D-galactoside alpha-2-L-fucosyltransferase is likely a counterpart of the human Secretor gene-encoded blood group transferase
J. Biol. Chem.
270
26577-26580
1995
Sus scrofa
brenda
Sherwood, A.L.; Stroud, M.R.; Levery, S.B.; Holmes, E.H.
An amino acid region at the N-terminus of rat hepatoma alpha1->2 fucosyltransferase modulates enzyme activity and interaction with lipids: strong preference for glycosphingolipids containing terminal Galbeta1->3GalNAc-structures
Biochemistry
40
5708-5719
2001