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Information on EC 2.4.1.69 - type 1 galactoside alpha-(1,2)-fucosyltransferase
for references in articles please use BRENDA:EC2.4.1.69
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.69 type 1 galactoside alpha-(1,2)-fucosyltransferase
IUBMB 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.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.4.1.69
-
fucosylation
- oligosaccharide
-
sialylated
- glycans
- glycosyltransferases
- epitope
- lectin
-
sialyltransferase
- glycolipids
- selectins
- glycoconjugates
-
histo-blood
-
n-acetylglucosaminyltransferase
-
fucts
-
e-selectin
-
nonsecretors
-
sialyl-lewis
- asialofetuin
- alpha-l-fucosidase
- xyloglucan
-
lewisa
-
hyperacute
-
fucosidase
- 2'-fucosyllactose
- n-acetyllactosamine
-
h-type
-
bombay
- lactosamine
-
xenoreactive
- psgl-1
-
fucose-containing
- fuct-vii
- analysis
-
difucosylated
- gnt-iii
-
hbgas
-
alpha1-6
- medicine
- noroviruses
-
1-3glcnac
-
xenoantigens
-
xylosyltransferase
-
glycomic
- lacnac
- synthesis
- neuac
- alpha-gal
-
alpha1,3-galactosyltransferase
- tamarind
- lacto-n-biose
Reaction Schemes
showSynonyms
fucosyltransferase, alpha1,2-fucosyltransferase, alpha(1,2)fucosyltransferase, fucosyltransferase 2, alpha1,2-ft, alpha(1,2)-fucosyltransferase, alpha-2-l-fucosyltransferase, fucosyltransferase 1, alpha-1,2-fucosyltransferase, alpha1,2ft, more
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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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-
-
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alpha-L-fucosyltransferase
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-
-
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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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-
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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 2
fucosyltransferase, guanosine diphosphofucose-galactoside 2-L-
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-
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fucosyltransferase, guanosine diphosphofucose-glycoprotein 2-alpha-
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fucosyltransferase, guanosine diphosphofucose-lactose
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-
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FucT
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FUT1
FUT2
futC
galactoside 2-alpha-L-fucosyltransferase
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-
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GDP fucose-lactose fucosyltransferase
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-
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GDP-beta-L-fucose:beta-D-galactosyl-R 2-alpha-L-fucosyltransferase
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-
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GDP-Fuc:beta-D-Gal alpha-1,2-fucosyltransferase
GDP-fucose:GM1 alpha1-2fucosyltransferase
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-
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GDP-L-fucose:beta-D-galactosyl-R-alpha-L-fucosyltransferase
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-
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GDP-L-fucose:lactose fucosyltransferase
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-
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GDPFuc:beta-D-galactoside alpha1,2-fucosyltransferase
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-
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guanosine diphospho-L-fucose-lactose fucosyltransferase
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-
-
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guanosine diphosphofucose-beta-D-galactosyl-alpha-2-L-fucosyltransferase
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-
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guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide alpha-L-fucosyltransferase
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-
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guanosine diphosphofucose-glycoprotein 2-alpha-L-fucosyltransferase
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-
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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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-
-
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HpfutC
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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-
-
-
CE2FT-2
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gene encoding an alpha1,2fucosyltransferase without activity towards Galbeta-O-p-nitrophenol or Galalpha-O-p-nitrophenol
GDP-Fuc:beta-D-Gal alpha-1,2-fucosyltransferase
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-
WbsJ
-
gene encoding an alpha1,2fucosyltransferase in Escherichia coli with a broad substrate specificity
WbsJ
-
gene encoding an alpha1,2fucosyltransferase in Escherichia coli with a broad substrate specificity
-
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
either a rapid equilibrium random kinetic mechanism or a steady state ordered mechanism with GDP-L-fucose binding first
-
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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-
-
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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
MetaCyc
ABH and Lewis epitopes biosynthesis from type 1 precursor disaccharide, biosynthesis of Lewis epitopes (H. pylori), lacto-series glycosphingolipids biosynthesis
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-beta-L-fucose +
?
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
?
GDP-beta-L-fucose + 2-nitrophenyl beta-D-galactopyranoside
GDP + 2-nitrophenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + 4-nitrophenyl-beta-lactose
GDP + 4-nitrophenyl-O-alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl(1->4)-D-glucopyranoside
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + anthranilyl-beta-lactose
GDP + anthranilyl-O-alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl(1->4)-D-glucopyranoside
-
Substrates: -
Products: -
Products: -
?
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-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-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-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-galactosamine
Substrates: residues of H type 3 epitopes, reaction of EC 2.4.1.69
Products: -
Products: -
?
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
Substrates: residues of H type 2 epitopes
Products: -
Products: -
?
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
-
Substrates: i.e. N-acetyllactosamine, reaction of EC 2.4.1.344
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + D-galactose
?
Substrates: 70% activity compared to D-lactose
Products: -
Products: -
?
GDP-beta-L-fucose + Gal(beta1-3)GlcNAc
?
Substrates: 28% activity compared to D-lactose
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta(1,3)GalNAcalpha-O-Me
GDP + ?
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta(1,3)GalNAcalpha-O-phenyl
GDP + ?
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta(1,4)Glcbeta-1-NAc
GDP + ?
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta(1,4)Glcbeta-N3
GDP + ?
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta(1,4)Glcbeta-O-phenyl
GDP + ?
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta(1,4)Glcbeta-S-phenyl
GDP + ?
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta(1-3)GalNAc
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAc
-
Substrates: -
Products: -
Products: -
ir
GDP-beta-L-fucose + Galbeta(1-3)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAc
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta(1-3)GalNAcalpha-O-p-nitrophenol
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAcalpha-O-p-nitrophenol
-
Substrates: -
Products: -
Products: -
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
-
Substrates: -
Products: -
Products: -
ir
GDP-beta-L-fucose + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc-beta-O-PA8
?
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta(1-3)GlcNAcbeta-O-p-nitrophenol
GDP + Fucalpha(1-2)Galbeta(1-3)GlcNAcbeta-O-p-nitrophenol
-
Substrates: activity is low
Products: -
Products: -
ir
GDP-beta-L-fucose + Galbeta(1-3)[Fucalpha(1-4)]GlcNAc
GDP + Fucalpha(1-2)Galbeta(1-3)[Fucalpha(1-4)]GlcNAc
-
Substrates: activity is low
Products: -
Products: -
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
-
Substrates: -
Products: -
Products: -
ir
GDP-beta-L-fucose + Galbeta-4-nitrophenyl
?
Substrates: 28% activity compared to D-lactose
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta-O-Me
GDP + L-Fucalpha(1-2)Galbeta-O-Me
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta-p-nitrophenol
GDP + L-Fucalpha(1-2)Galbeta-p-nitrophenol
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta1-3GlcNAc
GDP + ?
-
Substrates: the enzyme has a strict requirement for acceptor glycans with non-reducing terminal Galbeta1-3GlcNAc structures
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc
GDP + ?
-
Substrates: the enzyme has a strict requirement for acceptor glycans with non-reducing terminal Galbeta1-3GlcNAc structures
Products: -
Products: -
?
GDP-beta-L-fucose + Galbeta1-3GlcNAcbeta1-O-Me
GDP + ?
-
Substrates: the enzyme has a strict requirement for acceptor glycans with non-reducing terminal Galbeta1-3GlcNAc structures
Products: -
Products: -
?
GDP-beta-L-fucose + lactose
GDP + fucosyllactose
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + lactulose
GDP + 2'-fucosyl-D-lactulose
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + phenyl beta-D-galactopyranoside
GDP + phenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + phenyl beta-D-thiogalactopyranoside
GDP + phenyl L-fucosyl-alpha-(1->2)-beta-D-thiogalactopyranoside
-
Substrates: -
Products: -
Products: -
?
GDP-fucose + Galbeta-O-Bn
GDP + L-Fucalpha(1-2)Galbeta-O-Bn
-
Substrates: -
Products: -
Products: -
?
GDP-fucose + Galbeta1-4Glc
Fucalpha1-2Galbeta1-4Glc + GDP
-
Substrates: -
Products: -
Products: -
?
GDP-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
Fucalpha1-2Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc + GDP
-
Substrates: -
Products: -
Products: -
?
GDP-L-Fuc + XLLGXLLG-2-aminopyridine
GDP + alpha-L-fucosyl-XLLGXLLG-2-aminopyridine
Substrates: acceptor xyloglucan oligosaccharide carrying two repeated XLLG units plus 2-aminopyridine
Products: -
Products: -
?
GDP-L-fucose + 6-sulfoGalbeta(1-4)GlcNAcbeta-O-methyl
GDP + L-Fucalpha(1-2)6-sulfoGalbeta(1-4)GlcNAcbeta-O-methyl
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + agalacto-asialofetuin
GDP + alpha-L-fucosyl-1,2-agalacto-asialofetuin
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + arabinogalactan protein
?
-
Substrates: isoforms FUT4.1 and FUT 6 incorporate terminal alpha-L-fucose residues on the C-2 positions of adjacent arabinose residues of arabinogalactan proteins
Products: -
Products: -
?
GDP-L-fucose + asialo alpha1 acid glycoprotein
GDP + alpha-L-fucosyl-1,2-asialo alpha1 acid glycoprotein
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + asialofetuin
GDP + alpha-L-fucosyl-1,2-asialofetuin
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + beta-D-galactose-beta-O-2-(2-carbomethoxyethylthio)ethyl
?
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + beta-methyl-D-galactopyranoside
GDP + alpha-L-fucosyl-1,2-beta-methyl-D-galactopyranoside
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + bovine IgG diantennary glycopeptide
GDP + ?
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + D-fucose
GDP + alpha-L-fucosyl-1,2-D-fucose
-
Substrates: -
Products: -
Products: -
?
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 + fetuin triantennary asialoglycopeptide
GDP + ?
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + GalalphaCH3
GDP + L-Fucalpha(1-2)GalalphaCH3
-
Substrates: 0.1% of the activity with Galbeta1-3GalNAc
Products: -
Products: -
?
GDP-L-fucose + Galbeta(1-3)Ara
GDP + L-Fucalpha(1-2)Galbeta(1-3)Ara
-
Substrates: 3.3% of the activity with Galbeta1-3GalNAc
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + Galbeta(1-3)GalNAcbeta1-OCH2CH=CH2
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAcbeta1-OCH2CH=CH2
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: 84% of the activity with Galbeta1-3GalNAc
Products: -
Products: -
?
GDP-L-fucose + Galbeta(1-3)GlcNAcbeta-O-allyl/acrylamide copolymer
GDP + ?
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + Galbeta(1-3)GlcNAcbeta-O-benzyl
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAcbeta-O-benzyl
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + Galbeta(1-4)Glc
GDP + L-Fucalpha(1-2)Galbeta(1-4)Glc
-
Substrates: 4.2% of the activity with Galbeta1-3GalNAc
Products: -
Products: -
?
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
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-4)GlcNAc
GDP + L-Fucalpha(1-2)Galbeta(1-4)GlcNAc
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Substrates: 7.5% of the activity with Galbeta1-3GalNAc
Products: -
Products: -
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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
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Substrates: 2.8% of the activity with Galbeta(1-3)GalNAc
Products: -
Products: -
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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
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Substrates: -
Products: -
Products: -
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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
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-4)GlcNAcbeta-O-benzyl
GDP + L-Fucalpha(1-2)Galbeta(1-4)GlcNAcbeta-O-benzyl
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-4)Man
GDP + L-Fucalpha(1-2)Galbeta(1-4)Man
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Substrates: 2.7% of the activity with Galbeta1-3GalNAc
Products: -
Products: -
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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 + Galbeta-O-benzyl
GDP + L-Fucalpha(1-2)Galbeta-O-benzyl
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + GalbetaCH3
GDP + L-Fucalpha(1-2)GalbetaCH3
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Substrates: 2.6% of the activity with Galbeta1-3GalNAc
Products: -
Products: -
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GDP-L-fucose + intestinal glycoprotein
GDP + alpha-L-fucosyl-1,2-intestinal glycoprotein
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + lacto-N-fucopentaose II
GDP + ?
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + p-nitrophenyl beta-D-fucoside
GDP + alpha-L-fucosyl-1,2-nitrophenyl beta-D-fucoside
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Substrates: -
Products: -
Products: -
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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
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Substrates: -
Products: -
Products: -
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GDP-L-Gal + xyloglucan oligosaccharide
GDP + L-galactosyl-xyloglucan oligosaccharide
Substrates: -
Products: -
Products: -
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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
Substrates: residues of H type 3 epitopes, reaction of EC 2.4.1.69
Products: -
Products: -
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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
Substrates: residues of H type 3 epitopes
Products: -
Products: -
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GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
Substrates: residues of H type 1 epitopes, reaction of EC 2.4.1.69
Products: -
Products: -
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GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
Substrates: residues of H type 1 epitopes
Products: -
Products: -
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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
Substrates: -
Products: -
Products: -
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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
Substrates: -
Products: -
Products: -
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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
Substrates: -
Products: -
Products: -
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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
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Substrates: i.e. lacto-N-biose I, reaction of EC 2.4.1.69
Products: 82% of the activity with phenyl beta-D-galactopyranoside
Products: 82% of the activity with phenyl beta-D-galactopyranoside
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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
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Substrates: i.e. lacto-N-biose I
Products: -
Products: -
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GDP-beta-L-fucose + beta-lactose
GDP + 2'-fucosyllactose
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Substrates: -
Products: -
Products: -
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GDP-beta-L-fucose + beta-lactose
GDP + 2'-fucosyllactose
WP_026938579.1
Substrates: -
Products: -
Products: -
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GDP-beta-L-fucose + beta-lactose
GDP + 2'-fucosyllactose
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Substrates: -
Products: -
Products: -
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GDP-beta-L-fucose + beta-lactose
GDP + 2'-fucosyllactose
Helicobacter pylori ATCC 26695
WP_026938579.1
Substrates: -
Products: -
Products: -
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GDP-beta-L-fucose + beta-lactose
GDP + 2'-fucosyllactose
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Substrates: alpha1,2-fucosyltransferase from Helicobacter sp. 11S02629-2 exhibits high in vivo 2'-fucosyllactose productivity without the formation of byproducts difucosyl lactose and 3-fucosyllactose. The maximum 2'-fucosyllactose titer and yield reaches 11.13 g/l and 0.98 mol/mol of lactose, respectively, in shake-flask cultivation, both approaching the theoretical maximum value. In a 5 l fed-batch cultivation, the maximum 2'-fucosyllactose titer reaches 94.7 g/l extracellularly with a yield of 0.98 mol of 2'-fucosyllactose/mol of lactose and productivity of 1.14 g/l*h
Products: -
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GDP-beta-L-fucose + D-lactose
GDP + 2'-fucosyl-D-lactose
Substrates: 100% activity
Products: -
Products: -
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GDP-beta-L-fucose + D-lactose
GDP + 2'-fucosyl-D-lactose
Substrates: 100% activity
Products: -
Products: -
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GDP-beta-L-fucose + D-lactulose
GDP + 2'-fucosyl-D-lactulose
Substrates: 125% activity compared to D-lactose
Products: -
Products: -
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GDP-beta-L-fucose + D-lactulose
GDP + 2'-fucosyl-D-lactulose
Substrates: 125% activity compared to D-lactose
Products: -
Products: -
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GDP-beta-L-fucose + Gal(beta1-4)GlcNAc
?
Substrates: 85% activity compared to D-lactose
Products: -
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GDP-beta-L-fucose + Gal(beta1-4)GlcNAc
?
Substrates: 85% activity compared to D-lactose
Products: -
Products: -
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GDP-beta-L-fucose + Gal-beta-OR
GDP + L-Fucalpha(1-2)Galbeta-OR
Q5JBG3
Substrates: -
Products: -
Products: -
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GDP-beta-L-fucose + Gal-beta-OR
GDP + L-Fucalpha(1-2)Galbeta-OR
Q5JBG3
Substrates: -
Products: -
Products: -
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GDP-beta-L-fucose + Galbeta(1-3)GalNAcalpha-OMe
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAcalpha-OMe
Q5JBG3
Substrates: -
Products: -
Products: -
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GDP-beta-L-fucose + Galbeta(1-3)GalNAcalpha-OMe
GDP + Fucalpha(1-2)Galbeta(1-3)GalNAcalpha-OMe
Q5JBG3
Substrates: -
Products: -
Products: -
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GDP-beta-L-fucose + lacto-N-biose
?
Substrates: -
Products: -
Products: -
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GDP-beta-L-fucose + lacto-N-biose
?
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-beta-L-fucose + lacto-N-biose
?
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-beta-L-fucose + lacto-N-biose-O-methyl
?
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-beta-L-fucose + lacto-N-biose-O-methyl
?
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-beta-L-fucose + lacto-N-hexaose
?
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-beta-L-fucose + lacto-N-hexaose
?
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-beta-L-fucose + lacto-N-tetraose
?
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-beta-L-fucose + lacto-N-tetraose
?
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-beta-L-fucose + lactose
GDP + 2'-fucosyllactose
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-beta-L-fucose + lactose
GDP + 2'-fucosyllactose
Substrates: the enzyme is specific, or at least highly selective, for GPD-Fuc as donor substrate. Preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
Substrates: fut1, fut2, and sec1 genes encode proteins that only can alpha1,2-fucosylate type 3/4, GM1 and galacto-N-biose acceptors
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: 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
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: detailed characterization of specificity
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: the acid form of the enzyme is probably involved in glycoprotein synthesis in vivo
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: fucosyltransferase 1 may contribute to pathological prostatic growth
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: enzyme is involved in expression of blood group H, Lewis b from Lewis a and Globo H
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: the galactoside 2-alpha-L-fucosyltransferase gene determines the expression of terminal L-Fucalpha(1-2)Galbeta epitopes
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: fucosyltransferase 1 may contribute to pathological prostatic growth
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: 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
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
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Substrates: the enzyme forms exclusively L-Fucalpha(1-2)Gal linkage with a variety of acceptor substrates
Products: -
Products: -
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GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: -
Products: -
Products: -
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GDP-L-fucose + D-galactose
GDP + alpha-L-fucosyl-1,2-D-galactose
Substrates: -
Products: -
Products: -
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GDP-L-fucose + D-galactose
GDP + alpha-L-fucosyl-1,2-D-galactose
-
Substrates: -
Products: -
Products: -
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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
-
Substrates: -
Products: -
Products: -
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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
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Substrates: -
Products: -
Products: -
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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
-
Substrates: -
Products: -
Products: -
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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
-
Substrates: -
Products: -
Products: -
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GDP-L-fucose + fetuin
GDP + alpha-L-fucosyl-1,2-fetuin
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + fetuin
GDP + alpha-L-fucosyl-1,2-fetuin
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + galacto-N-biose
GDP + alpha-L-fucosyl-1,2-galacto-N-biose
Substrates: -
Products: -
Products: -
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GDP-L-fucose + galacto-N-biose
GDP + alpha-L-fucosyl-1,2-galacto-N-biose
Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-2)D-Xyl
GDP + L-Fucalpha(1-2)D-Galbeta(1-2)D-Xyl
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-2)D-Xyl
GDP + L-Fucalpha(1-2)D-Galbeta(1-2)D-Xyl
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-2)D-Xyl
GDP + L-Fucalpha(1-2)D-Galbeta(1-2)D-Xyl
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-2)D-Xyl
GDP + L-Fucalpha(1-2)D-Galbeta(1-2)D-Xyl
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-3)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAc
-
Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-3)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAc
-
Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-3)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAc
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-6)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-6)GalNAc
-
Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1-6)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-6)GalNAc
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Substrates: 4.8% of the activity with Galbeta1-3GalNAc
Products: -
Products: -
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GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OH
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OH
Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OH
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OH
Substrates: -
Products: -
Products: -
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GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OMe
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OMe
Substrates: highest activity
Products: -
Products: -
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GDP-L-fucose + Galbeta(1->3)-GalNAcalpha-OMe
GDP + Fucalpha(1->2)-Galbeta(1->3)-GalNAcalpha-OMe
Substrates: highest activity
Products: -
Products: -
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GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
Substrates: -
Products: -
Products: -
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GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
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Substrates: -
Products: -
Products: -
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GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
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Substrates: i.e. Gal(1-3)GlcNAc
Products: -
Products: -
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lacto-N-neotetraose
GDP + lacto-N-fucopentaose IV
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lacto-N-neotetraose
GDP + lacto-N-fucopentaose IV
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lacto-N-tetraose
GDP + lacto-N-fucopentaose I
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lacto-N-tetraose
GDP + lacto-N-fucopentaose I
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lacto-N-tetraose
GDP + lacto-N-fucopentaose I
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lactose
GDP + fucosyllactose
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + lactose
GDP + fucosyllactose
-
Substrates: -
Products: 2'-fucosyllactose
Products: 2'-fucosyllactose
?
GDP-L-fucose + lactose
GDP + fucosyllactose
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucosyl-1,2-N-acetyllactosamine
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucosyl-1,2-N-acetyllactosamine
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucosyl-1,2-N-acetyllactosamine
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucosyl-1,2-N-acetyllactosamine
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: dearabinosylated arabinogalactan proteins are not substrate acceptors for isoforms FUT4.1 and FUT6
Products: -
Products: -
?
additional information
?
-
Substrates: recombinant FUT1 catalyzes L-Gal transfer to xyloglucan oligosaccharides with an initial velocity of L-Gal transfer 3.1 times lower than that of L-Fuc transfer. No acceptor: mono-D-galactosylated xyloglucan oligosaccharide XXLG-2-aminopyridine, XLLG-2-aminopyridine
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme favors certain glycoproteins containing polylactosamine units
Products: -
Products: -
?
additional information
?
-
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme reduces terminal alpha(2,3)-sialylation in transfected cells and transgenic animals
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: FUT2 directs alpha2-fucosylation on type 1 chains on both N- and O-linked glycan structures
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: FutC substrates are generated by both FutA and FutB, and their heptad repeat number correlates to Lewis y O-antigen polymer sizes
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 4-nitrophenyl-alpha-Gal, P-alpha-Glc, 4-nitrophenyl-beta-GalNAc, 4-nitrophenyl-beta-Gal, 4-nitrophenyl-beta-Glc, 4-nitrophenyl-alpha-GlcNAc, and 4-nitrophenyl-beta-GlcNAc
Products: -
Products: -
-
additional information
?
-
P97327
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
additional information
?
-
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows a strong preference for terminal Galbeta1, 3GalNAc structures
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: residues of H type 3 epitopes, reaction of EC 2.4.1.69
Products: -
Products: -
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
Substrates: residues of H type 1 epitopes, reaction of EC 2.4.1.69
Products: -
Products: -
?
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-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-galactosamine
Substrates: residues of H type 3 epitopes, reaction of EC 2.4.1.69
Products: -
Products: -
?
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
Substrates: residues of H type 2 epitopes
Products: -
Products: -
?
GDP-beta-L-fucose + beta-lactose
GDP + 2'-fucosyllactose
-
Substrates: -
Products: -
Products: -
?
GDP-beta-L-fucose + phenyl beta-D-galactopyranoside
GDP + phenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
Substrates: -
Products: -
Products: -
?
GDP-fucose + Galbeta1-4Glc
Fucalpha1-2Galbeta1-4Glc + GDP
-
Substrates: -
Products: -
Products: -
?
GDP-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
Fucalpha1-2Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc + GDP
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: -
Products: -
Products: -
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: the acid form of the enzyme is probably involved in glycoprotein synthesis in vivo
Products: -
Products: -
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: fucosyltransferase 1 may contribute to pathological prostatic growth
Products: -
Products: -
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: enzyme is involved in expression of blood group H, Lewis b from Lewis a and Globo H
Products: -
Products: -
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: the galactoside 2-alpha-L-fucosyltransferase gene determines the expression of terminal L-Fucalpha(1-2)Galbeta epitopes
Products: -
Products: -
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
Substrates: fucosyltransferase 1 may contribute to pathological prostatic growth
Products: -
Products: -
?
additional information
?
-
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: FUT2 directs alpha2-fucosylation on type 1 chains on both N- and O-linked glycan structures
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: FutC substrates are generated by both FutA and FutB, and their heptad repeat number correlates to Lewis y O-antigen polymer sizes
Products: -
Products: -
?
additional information
?
-
P97327
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
additional information
?
-
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Mg2+
Mn2+
additional information
Ba2+
-
10 mM, enzyme from gastric mucosa: 6.3% of the activation with Mn2+, enzyme from plasma: 108% of the activation with Mn2+
Ca2+
-
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, 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, 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+
WP_026938579.1
the enzyme activity is highest at a final concentration of 4 mM of Mn2+ and decreases as the concentration continues to increase
Mn2+
-
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
the L-galactosyltransferase activity of Fut1 is found in the absence of divalent cations and in the presence of EDTA
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+
additional information
-
enzymatic reaction of the CgFUT2 is not dependent on divalent cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetonitrile
-
addition of 5%, 10% and 15% of acetonitrile decrease the activity by 48%, 58% and 65% respectively
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
methanol
-
presence of 5%, 10% and 15% of methanol decrease the activity by 14%, 21% and 41% respectively
2-mercaptoethanol
-
complete inhibition of activity with lacto-N-biose I
additional information
the L-galactosyltransferase activity of Fut1 is found in the absence of divalent cations and in the presence of EDTA
-
additional information
-
presence of EDTA does not abolish the transfer activity
-
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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
3.8
beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
pH 7.2, 37°C
11.1
beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
pH 7.2, 37°C
7.1
beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
pH 7.2, 37°C
8.3
beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
pH 7.2, 37°C
0.95
beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
-
pH 7.2, temperature not specified in the publication
0.04778
beta-lactose
-
pH 7.5, 37°C, mutant enzyme D115F/G172R/G174A/Q176L/G178H/I179Y/H269W/H274G/T348S
0.36
beta-lactose
WP_026938579.1
pH 5.0, 37°C, mutant enzyme K102T/R105C/D115S/Y251F/A255G/K282E
0.00726
GDP-beta-L-fucose
-
pH 7.5, 37°C, mutant enzyme D115F/G172R/G174A/Q176L/G178H/I179Y/H269W/H274G/T348S
0.06
GDP-beta-L-fucose
WP_026938579.1
pH 5.0, 37°C, mutant enzyme K102T/R105C/D115S/Y251F/A255G/K282E
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
-
wild type isoform FUT1, in 50 mM Tris-HCl (pH 7.2), at 37°C
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
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
0.163
beta-lactose
WP_026938579.1
pH 5.0, 37°C, mutant enzyme K102T/R105C/D115S/Y251F/A255G/K282E
0.32
beta-lactose
-
pH 7.5, 37°C, mutant enzyme D115F/G172R/G174A/Q176L/G178H/I179Y/H269W/H274G/T348S
0.075
GDP-beta-L-fucose
-
pH 7.5, 37°C, mutant enzyme D115F/G172R/G174A/Q176L/G178H/I179Y/H269W/H274G/T348S
0.143
GDP-beta-L-fucose
WP_026938579.1
pH 5.0, 37°C, mutant enzyme K102T/R105C/D115S/Y251F/A255G/K282E
0.011
phenyl-beta-D-galactoside
-
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
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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
0.452
beta-lactose
WP_026938579.1
pH 5.0, 37°C, mutant enzyme K102T/R105C/D115S/Y251F/A255G/K282E
6.7
beta-lactose
-
pH 7.5, 37°C, mutant enzyme D115F/G172R/G174A/Q176L/G178H/I179Y/H269W/H274G/T348S
2.38
GDP-beta-L-fucose
WP_026938579.1
pH 5.0, 37°C, mutant enzyme K102T/R105C/D115S/Y251F/A255G/K282E
10.33
GDP-beta-L-fucose
-
pH 7.5, 37°C, mutant enzyme D115F/G172R/G174A/Q176L/G178H/I179Y/H269W/H274G/T348S
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
0.873
2.22
WP_026938579.1
pH 5.0, 37°C, mutant enzyme K102T/R105C/D115S/Y251F/A255G
2.3
WP_026938579.1
pH 5.0, 37°C, mutant enzyme K102T/R105C/D115S/Y251F/A255G/K282E
additional information
0.852
Q5JBG3
activity of WbwK-GST fusion protein with Galbeta1,3GalNAcalpha-O-benzyl as substrate
0.852
Q5JBG3
activity of WbwK-GST fusion protein with Galbeta(1-3)GalNAcalpha-O-benzyl as substrate
0.873
Q5JBG3
activity of WbwK-GST fusion protein with Galbeta1,3GalNAcalpha-O-methyl as substrate
0.873
Q5JBG3
activity of WbwK-GST fusion protein with Galbeta(1-3)GalNAcalpha-O-methyl as substrate
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
4.5 - 7
WP_026938579.1
pH 4.5: about 50% of maximal activity, pH 7.0: about 45% of maximal activity, wild-type enzyme
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
37
40
WP_026938579.1
mutant enzymes K102T, Y251F, K282E, Y251F/A255G/K282E, K102T/R105C/D115S/Y251F/A255G and K102T/R105C/D115S/Y251F/A255G/K282E
37
WP_026938579.1
wild-type enzyme and mutant enzymes D115S, K102T/R105C, K102T/R105C/D115S and Y251F/A255G
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16 - 30
-
16°C: 61% of maximal activity, 30°C: 62% of maximal activity
30 - 45
WP_026938579.1
the relative activity of wild-type enzyme and the mutants exceedes 60% in the range of 30-45°C. The wild-type enzyme does not show enzymatic activity at temperatures above 50°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
349720, 489348, 489349, 489350, 489351, 489352, 489359, 489360, 489361, 489363, 489365, 657489, 657509
-
-
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
-
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
additional information
-
no cDNA detected in urinary bladder, the testis, the seminal vesicle, the ovary, the uterus, the spleen, the brain or muscle
brenda
additional information
no cDNA detected in urinary bladder, the testis, the seminal vesicle, the ovary, the uterus, the spleen, the brain or muscle
brenda
additional information
no cDNA detected in urinary bladder, the testis, the seminal vesicle, the ovary, the uterus, the spleen, the brain or muscle
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme localizes to either outer membrane or inner compartments of the parasite mitochondrion
brenda
-
the enzyme localizes to either outer membrane or inner compartments of the parasite mitochondrion
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
physiological function
additional information
-
he expression ofFucT2 mutants using KanR as the phenotypical reporter leads to a significant increase in the production titer and yield of 2'-fucosyllactose in Escherichia coli
drug target
mitochondrial fucosyltransferase activity may have therapeutic potential across trypanosomatids
drug target
-
mitochondrial fucosyltransferase activity may have therapeutic potential across trypanosomatids
-
malfunction
the spontaneous G428A nonsense mutation in FUT2 provides strong but not absolute protection against symptomatic GII.4 Norovirus infection
malfunction
-
absence of pgtA, wild-type O2 dependence of culmination
malfunction
blocking enzyme expression in arthritis synovial fibroblasts reduces endothelial cell tube formation
metabolism
-
in roots, isoforms FUT4 and FUT6 genes are responsible for arabinogalactan fucosylation
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
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
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.
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
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.
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.
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
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
the enzyme is required for mitochondrial function in bloodstream form trypanosomes
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.
-
physiological function
-
the enzyme is required for mitochondrial function in bloodstream form trypanosomes
-
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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). A6M9C2_ECOLX
297
0
34942
TrEMBL
Chloroplast (Reliability: 5)
FUT1_HUMAN
365
1
41251
Swiss-Prot
Secretory Pathway (Reliability: 2)
SEC1_MOUSE
368
0
41464
Swiss-Prot
other Location (Reliability: 1)
Q38FH1_TRYB2
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
308
0
35242
TrEMBL
-
Q5J7C6_ECOLX
299
0
35048
TrEMBL
Secretory Pathway (Reliability: 4)
FUT2_HYLLA
343
1
39059
Swiss-Prot
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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 * 61000, His-tagged isoform FUT4.1, calculated from amino acid sequence
?
-
x * 59000, His-tagged isoform FUT6, calculated from amino acid sequence
?
x * 70000, recombinant, His- and pro-protein-tagged enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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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
A255G
WP_026938579.1
t1/2 value at 40°C is 0.41 h (wild-type value is 0.4 h)
D115F/G172R/G174A/Q176L/G178H/I179Y/H269W/H274G/T348S
-
the achieve strict substrate selectivity and high substrate tolerance semi-rational manipulation combining computer-aided designing and screening with biochemical experiments are adopted. The mutant has a 100fold increase in catalytic efficiency compared to the wild-type. The highest 2'-fucosyllactose yield was up to 0.65 mol/mol lactose with a productivity of 2.56 g ml/l*h performed by enzymatic catalysis in vitro. Further analysis reveales that the interactions between the mutant and substrates are reduced
D115S
WP_026938579.1
t1/2 value at 40°C is 0.43 h (wild-type value is 0.4 h)
K102T
WP_026938579.1
t1/2 value at 40°C is 0.49 h (wild-type value is 0.4 h)
K102T/R105C
WP_026938579.1
specific activity is 2.72fold higher than the wild-type value
K102T/R105C/D115S
WP_026938579.1
specific activity of the mutant enzyme is 2.9fold higher than the wild-type value
K102T/R105C/D115S/Y251F/A255G
WP_026938579.1
specific activity of the mutant enzyme is 3.13fold higher than the wild-type value
K102T/R105C/D115S/Y251F/A255G/K282E
WP_026938579.1
specific activity of the mutant enzyme is 3.2fold higher than the wild-type valuet. 1/2 value at 40°C is 0.87 h (wild-type value is 0.4 h)
K282E
WP_026938579.1
t1/2 value at 40°C is 0.48 h (wild-type value is 0.4 h)
R105C
WP_026938579.1
t1/2 value at 40°C is 0.39 h (wild-type value is 0.4 h)
Y251F
WP_026938579.1
t1/2 value at 40°C is 0.45 h (wild-type value is 0.4 h)
Y251F/A255G
WP_026938579.1
specific activity of the mutant enzyme is 2.4fold higher than the wild-type value
Y251F/A255G/K282E
WP_026938579.1
specific activity of the mutant enzyme is 2.75fold higher than the wild-type value
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
-
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
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.
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.
-
additional information
WP_026938579.1
semi-rationally designed site-saturation mutation is applied to engineer the catalytic activity and thermostability of HpfutC
additional information
Helicobacter pylori ATCC 26695
-
semi-rationally designed site-saturation mutation is applied to engineer the catalytic activity and thermostability of HpfutC
-
additional information
-
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
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
-
bp428 G>A is a spontaneous nonsense mutation, 739G > A substitution does not inactivate the enzyme
additional information
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
WP_026938579.1
12 h, residual enzyme activity of wild-type HpfutC maintains 70% of the original enzyme activity between pH 5.0 and 6.0
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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
37
40
WP_026938579.1
t1/2 value for the wild-type enzyme: 0.4 h. t1/2 values for mutants K102T, R105C, D115S, Y251F, A255G, K282E and K102T/R105C/D115S/Y251F/A255G/K282E are 0.49 h, 0.39 h, 0.43 h, 0.45 h, 0.41 h, 0.48 h and 0.87 h (in presence of 2 mM Mn2+)
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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
expressed as full-length protein with and without a C-terminal HPC4-epitope tag in human 293T cells
-
expression in Escherichia coli
expression in Escherichia coli BL21(DE3). The maximum 2'-fucosyllactose titer and yield reaches 11.13 g/l and 0.98 mol/mol of lactose, respectively, in shake-flask cultivation, both approaching the theoretical maximum value. In a 5 l fed-batch cultivation, the maximum 2'-fucosyllactose titer reaches 94.7 g/l extracellularly with a yield of 0.98 mol of 2'-fucosyllactose/mol of lactose and productivity of 1.14 g/l*h
-
expression in Escherichia coli. The expression ofFucT2 mutants using KanR as the phenotypical reporter leads to a significant increase in the production titer and yield of 2'-fucosyllactose in Escherichia coli
-
full length enzyme and truncated enzyme missing the first 27 amino acid residues from the N-terminus, comprising the cytoplasmic and transmembrane domains
overexpression of TcFUT1 with a C-terminal 6xMyc epitope tag in Trypanosoma cruzi epimastigote cells
-
porcine endothelial cell line transfected with human alpha(1,2)-fucosyltransferase cDNA
-
subcloned in COS-7 or CHOP cells (Chinese hamster ovary cells transformed with Polyoma large T antigen)
-
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
-
the wbsJ gene is overexpressed in Escherichia coli BL21 as a fusion protein with glutathione S-transferase (GST) at its N-terminus
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold 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 2030fold 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 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
P97327, Q9JL27
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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)
-
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
food industry
-
2'-fucosyllactose, a representative oligosaccharide in human milk, is an emerging and promising food and pharmaceutical ingredient due to its powerful health benefits, such as participating in immune regulation, regulation of intestinal flora, etc. To enable economically viable production of 2'-fucosyllactose, different biosynthesis strategies using precursors and pathway enzymes are developed. The alpha-1,2-fucosyltransferases are an essential part involved in these strategies, but their strict substrate selectivity and unsatisfactory substrate tolerance are one of the key roadblocks limiting biosynthesis
industry
medicine
pharmacology
-
2'-fucosyllactose, a representative oligosaccharide in human milk, is an emerging and promising food and pharmaceutical ingredient due to its powerful health benefits, such as participating in immune regulation, regulation of intestinal flora, etc. To enable economically viable production of 2'-fucosyllactose, different biosynthesis strategies using precursors and pathway enzymes are developed. The alpha-1,2-fucosyltransferases are an essential part involved in these strategies, but their strict substrate selectivity and unsatisfactory substrate tolerance are one of the key roadblocks limiting biosynthesis
synthesis
industry
WP_026938579.1
the enzyme has great potential for industrial 2'-fucosyllactose production
industry
Helicobacter pylori ATCC 26695
-
the enzyme has great potential for industrial 2'-fucosyllactose production
-
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
-
tumor marker for human gastric cancer, down regulation of alpha1,2-fucosyltransferase activity is associated with human gastric tumorigenesis
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
-
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
-
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
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
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
synthesis
-
introduction of the WcfB gene plus the genes for guanosine 5'-diphosphate-L-fucose biosynthetic enzymes allows the lacZ-deleted Escherichia coli to produce 2-fucosyllactose. By fedbatch fermentation, 15.4 g/l (extracellular concentration) of 2-fucosyllactose can be obtained (yield of 0.858 g/g lactose and productivity of 0.530 g/l/h)
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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 (Q28113), Bos taurus
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
Rattus norvegicus (Q10984)
brenda
Prieto, P.A.; Larsen, R.D.; Cho, M.; Rivera, H.N.; Shilatifard, A.; Lowe, J.B.; Cummings, R.D.; Smith, D.F.
Expression of human H-type alpha1,2-fucosyltransferase encoding for blood group H(O) antigen in Chinese hamster ovary cells. Evidence for preferential fucosylation and truncation of polylactosamine sequences
J. Biol. Chem.
272
2089-2097
1997
Homo sapiens
brenda
Domino, S.E.; Hiraiwa, N.; Lowe, J.B.
Molecular cloning, chromosomal assignment and tissue-specific expression of a murine alpha-(1,2)fucosyltransferase expressed in thymic and epididymal epithelial cells
Biochem. J.
327
105-115
1997
Homo sapiens, Mus musculus
-
brenda
Masutani, H.; Kimura, H.
Purification and characterization of secretory-type GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase from human gastric mucosa
J. Biochem.
118
541-545
1995
Homo sapiens
brenda
Marker, P.C.; Stephan, J.P.; Lee, J.; Bald, L.; Mather, J.P.; Cunha, G.R.
Fucosyltransferase1 and H-type complex carbohydrates modulate epithelial cell proliferation during prostatic branching morphogenesis
Dev. Biol.
233
95-108
2001
Homo sapiens, Rattus norvegicus
brenda
Karaivanova, V.; Mookerjea, S.; Hunt, D.; Nagpurkar, A.
Characterization and purification of fucosyltransferases from the cytosol of rat colon
Int. J. Biochem. Cell Biol.
28
165-174
1996
Rattus norvegicus
brenda
Chandrasekaran, E.V.; Chawda, R.; Locke, R.D.; Piskorz, C.F.; Matta, K.L.
Biosynthesis of the carbohydrate antigenic determinants, Globo H, blood group H, and Lewis b: a role for prostate cancer cell alpha1,2-L-fucosyltransferase
Glycobiology
12
153-162
2002
Homo sapiens
brenda
Trinchera, M.; Bozzaro, S.
Dictyostelium cytosolic fucosyltransferase synthesizes H type 1 trisaccharide in vitro
FEBS Lett.
395
68-72
1996
Dictyostelium discoideum
brenda
Koda, Y.; Soejima, M.; Kimura, H.
Changing transcription start sites in H-type alpha(1,2)fucosyltransferase gene (FUT1) during differentiation of the human erythroid lineage
Eur. J. Biochem.
256
379-387
1998
Homo sapiens
brenda
Mulder, H.; Schachter, H.; Thomas, J.R.; Halkes, K.M.; Kamerling, J.P.; Vliegenthart, J.F.
Identification of a GDP-Fuc:Gal beta 1-3GalNAc-R (Fuc to Gal) alpha 1-2 fucosyltransferase and a GDP-Fuc:Gal beta 1-4GlcNAc (Fuc to GlcNAc) alpha 1-3 fucosyltransferase in connective tissue of the snail Lymnaea stagnalis
Glycoconjugate J.
13
107-113
1996
Lymnaea stagnalis
brenda
Druzhinina, T.N.; Sizova, O.V.; Shibaev, V.N.
Fucosylation of synthetic oligosaccharides - plant xyloglucan fragments - by mammalian and amphibian fucosyltransferases
Biochemistry (Moscow)
62
62-65
1997
Sus scrofa, Rattus norvegicus, Xenopus laevis, Rana temporaria
brenda
Chandrasekaran, E.V.; Jain, R.K.; Larsen, R.D.; Wlasichuk, K.; Matta, K.L.
Characterization of the specificities of human blood group H gene-specified alpha1,2-L-fucosyltransferase toward sulfated/sialylated/fucosylated acceptors: evidence for an inverse relationship between alpha1,2-L-fucosylation of Gal and alpha1,6-L-fucosylation of asparagine-linked GlcNAc
Biochemistry
35
8914-8924
1996
Homo sapiens
brenda
Bureau, V.; Marionneau, S.; Cailleau-Thomas, A.; Le Moullac-Vaidye, B.; Liehr, T.; Le Pendu, J.
Comparison of the three rat GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferases FTA, FTB and FTC
Eur. J. Biochem.
268
1006-1019
2001
Rattus norvegicus, Rattus norvegicus (Q10980), Rattus norvegicus (Q10984)
brenda
Yan, J.L.; Yu, L.Y.; Guo, L.H.
Human alpha galactosidase and alpha 1,2 fucosyltransferase concordantly inhibit xenoreactivity of NIH 3T3 cells with human serum
Acta Pharmacol. Sin.
24
878-884
2003
Homo sapiens
brenda
Mathieu, S.; Prorok, M.; Benoliel, A.M.; Uch, R.; Langlet, C.; Bongrand, P.; Gerolami, R.; El-Battari, A.
Transgene expression of alpha(1,2)-fucosyltransferase-I (FUT1) in tumor cells selectively inhibits sialyl-lewis x expression and binding to E-selectin without affecting synthesis of sialyl-Lewis a or binding to P-selectin
Am. J. Pathol.
164
371-383
2004
Homo sapiens
brenda
Serpa, J.; Mendes, N.; Reis, C.A.; Santos Silva, L.F.; Almeida, R.; Le Pendu, J.; David, L.
Two new FUT2 (fucosyltransferase 2 gene) missense polymorphisms, 739G-->A and 839T-->C, are partly responsible for non-secretor status in a Caucasian population from Northern Portugal
Biochem. J.
383
469-474
2004
Homo sapiens
brenda
Iwamori, M.; Tanaka, K.; Kubushiro, K.; Lin, B.; Kiguchi, K.; Ishiwata, I.; Tsukazaki, K.; Nozawa, S.
Alterations in the glycolipid composition and cellular properties of ovarian carcinoma-derived RMG-1 cells on transfection of the alpha1,2-fucosyltransferase gene
Cancer Sci.
96
26-30
2005
Mus musculus (P97327), Mus musculus (Q9JL27), Mus musculus, Homo sapiens (P19526), Homo sapiens
brenda
Shao, J.; Li, M.; Jia, Q.; Lu, Y.; Wang, P.G.
Sequence of Escherichia coli O128 antigen biosynthesis cluster and functional identification of an alpha-1,2-fucosyltransferase
FEBS Lett.
553
99-103
2003
Escherichia coli (Q6XQ53), Escherichia coli
brenda
Sepp, A.; Skacel, P.; Lindstedt, T.; Lechler, R.I.
Expression of alpha(1,3)galactose and other type 2 oligosaccharide structures in a porcine endothelial cell line transfected with human alpha(1,2)-fucosyltransferase cDNA
J. Biol. Chem.
272
23104-23110
1997
Homo sapiens
brenda
Kindberg, E.; Hejdeman, B.; Bratt, G.; Wahren, B.; Lindblom, B.; Hinkula, J.; Svensson, L.
A nonsense mutation (428G-->A) in the fucosyltransferase FUT2 gene affects the progression of HIV-1 infection
AIDS
20
685-689
2006
Homo sapiens
brenda
Drouillard, S.; Driguez, H.; Samain, E.
Large-scale synthesis of H-antigen oligosaccharides by expressing Helicobacter pylori alpha1,2-fucosyltransferase in metabolically engineered Escherichia coli cells
Angew. Chem.
45
1778-1780
2006
Helicobacter pylori
brenda
Park, K.U.; Song, J.; Han, K.S.; Kim, J.Q.
The fusion allele of the FUT2 (secretor type alpha(1,2)-fucosyltransferase) gene at a high frequency and a new se385 allele in a Korean population
Ann. Hematol.
84
656-660
2005
Homo sapiens
brenda
Scheppokat, A.M.; Bretting, H.; Thiem, J.
Fast and efficient synthesis of a novel homologous series of L-fucosylated trisaccharides using the Helix pomatia alpha-(1->2)-L-galactosyltransferase
Carbohydr. Res.
338
2083-2090
2003
Helix pomatia
brenda
Holgersson, J.; Loefling, J.
Glycosyltransferases involved in type 1 chain and Lewis antigen biosynthesis exhibit glycan and core chain specificity
Glycobiology
16
584-593
2006
Homo sapiens
brenda
Chandrasekaran, E.V.; Xue, J.; Piskorz, C.; Locke, R.D.; Toth, K.; Slocum, H.K.; Matta, K.L.
Potential tumor markers for human gastric cancer: an elevation of glycan:sulfotransferases and a concomitant loss of alpha1,2-fucosyltransferase activities
J. Cancer Res. Clin. Oncol.
133
599-611
2007
Homo sapiens
brenda
Thorven, M.; Grahn, A.; Hedlund, K.O.; Johansson, H.; Wahlfrid, C.; Larson, G.; Svensson, L.
A homozygous nonsense mutation (428G-->A) in the human secretor (FUT2) gene provides resistance to symptomatic norovirus (GGII) infections
J. Virol.
79
15351-15355
2005
Homo sapiens
brenda
Nilsson, C.; Skoglund, A.; Moran, A.P.; Annuk, H.; Engstrand, L.; Normark, S.
An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection
Proc. Natl. Acad. Sci. USA
103
2863-2868
2006
Homo sapiens
brenda
Meng, D.; Newburg, D.S.; Young, C.; Baker, A.; Tonkonogy, S.L.; Sartor, R.B.; Walker, W.A.; Nanthakumar, N.N.
Bacterial symbionts induce a FUT2-dependent fucosylated niche on colonic epithelium via ERK and JNK signaling
Am. J. Physiol. Gastrointest. Liver Physiol.
293
G780-G787
2007
Homo sapiens
brenda
Soejima, M.; Koda, Y.
Distinct single nucleotide polymorphism pattern at the FUT2 promoter among human populations
Ann. Hematol.
87
19-25
2008
Homo sapiens
brenda
Li, M.; Liu, X.W.; Shao, J.; Shen, J.; Jia, Q.; Yi, W.; Song, J.K.; Woodward, R.; Chow, C.S.; Wang, P.G.
Characterization of a novel alpha1,2-fucosyltransferase of Escherichia coli O128:b12 and functional investigation of its common motif
Biochemistry
47
378-387
2008
Escherichia coli
brenda
Mathieu, S.; Gerolami, R.; Luis, J.; Carmona, S.; Kol, O.; Crescence, L.; Garcia, S.; Borentain, P.; El-Battari, A.
Introducing alpha(1,2)-linked fucose into hepatocarcinoma cells inhibits vasculogenesis and tumor growth
Int. J. Cancer
121
1680-1689
2007
Homo sapiens
brenda
Moehler, T.M.; Sauer, S.; Witzel, M.; Andrulis, M.; Garcia-Vallejo, J.J.; Grobholz, R.; Willhauck-Fleckenstein, M.; Greiner, A.; Goldschmidt, H.; Schwartz-Albiez, R.
Involvement of alpha 1-2-fucosyltransferase I (FUT1) and surface-expressed Lewis(y) (CD174) in first endothelial cell-cell contacts during angiogenesis
J. Cell. Physiol.
215
27-36
2008
Homo sapiens
brenda
Yip, S.P.; Lai, S.K.; Wong, M.L.
Systematic sequence analysis of the human fucosyltransferase 2 (FUT2) gene identifies novel sequence variations and alleles
Transfusion
47
1369-1380
2007
Homo sapiens (Q10981), Homo sapiens
brenda
Li, M.; Shen, J.; Liu, X.; Shao, J.; Yi, W.; Chow, C.S.; Wang, P.G.
Identification of a new alpha1,2-fucosyltransferase involved in O-antigen biosynthesis of Escherichia coli O86:B7 and formation of H-type 3 blood group antigen
Biochemistry
47
11590-11597
2008
Escherichia coli, Escherichia coli (Q5JBG3), Escherichia coli O86:B7, Escherichia coli O86:B7 (Q5JBG3)
brenda
Zheng, Q.; Van Die, I.; Cummings, R.D.
A novel alpha1,2-fucosyltransferase (CE2FT-2) in Caenorhabditis elegans generates H-type 3 glycan structures
Glycobiology
18
290-302
2008
Caenorhabditis elegans
brenda
Silva, L.M.; Carvalho, A.S.; Guillon, P.; Seixas, S.; Azevedo, M.; Almeida, R.; Ruvoen-Clouet, N.; Reis, C.A.; Le Pendu, J.; Rocha, J.; David, L.
Infection-associated FUT2 (Fucosyltransferase 2) genetic variation and impact on functionality assessed by in vivo studies
Glycoconj. J.
27
61-68
2010
Homo sapiens
brenda
Wang, Z.A.; van der Wel, H.; Vohra, Y.; Buskas, T.; Boons, G.J.; West, C.M.
Role of a cytoplasmic dual-function glycosyltransferase in O2 regulation of development in Dictyostelium
J. Biol. Chem.
284
28896-28904
2009
Dictyostelium discoideum
brenda
Abrantes, J.; Posada, D.; Guillon, P.; Esteves, P.J.; Le Pendu, J.
Widespread gene conversion of alpha-2-fucosyltransferase genes in mammals
J. Mol. Evol.
69
22-31
2009
Bos taurus (Q9TTY3), Bos taurus (A4IFH1), Bos taurus (Q28113), Chlorocebus sabaeus, Chlorocebus sabaeus (O77711), Chlorocebus sabaeus (O77712), Gorilla gorilla (Q9TUD4), Gorilla gorilla (O77486), Homo sapiens (P19526), Homo sapiens (Q10981), Homo sapiens (Q5XLR8), Homo sapiens, Hylobates agilis (Q6LA46), Hylobates lar (Q9TTC7), Macaca fascicularis (Q9N266), Monodelphis domestica, Mus musculus (O09160), Mus musculus (P97353), Oryctolagus cuniculus (Q10983), Oryctolagus cuniculus (Q29505), Oryctolagus cuniculus (Q10979), Oryctolagus cuniculus, Pan troglodytes (O77485), Pan troglodytes (Q9TUD6), Pongo pygmaeus (Q6LA45), Pongo pygmaeus (O77487), Rattus norvegicus (Q9WUE6), Rattus norvegicus (Q10980), Rattus norvegicus (Q10984), Sus scrofa (Q10982), Sus scrofa (Q29043), Xenopus tropicalis
brenda
Christiansen, D.; Milland, J.; Dodson, H.C.; Lazarus, B.D.; Sandrin, M.S.
The cytoplasmic and transmembrane domains of secretor type alpha1,2fucosyltransferase confer atypical cellular localisation
J. Mol. Recognit.
22
250-254
2009
Sus scrofa
brenda
Hazra, A.; Kraft, P.; Selhub, J.; Giovannucci, E.L.; Thomas, G.; Hoover, R.N.; Chanock, S.J.; Hunter, D.J.
Common variants of FUT2 are associated with plasma vitamin B12 levels
Nat. Genet.
40
1160-1162
2008
Homo sapiens (Q10981)
brenda
Carlsson, B.; Kindberg, E.; Buesa, J.; Rydell, G.E.; Lidon, M.F.; Montava, R.; Abu Mallouh, R.; Grahn, A.; Rodriguez-Diaz, J.; Bellido, J.; Arnedo, A.; Larson, G.; Svensson, L.
The G428A nonsense mutation in FUT2 provides strong but not absolute protection against symptomatic GII.4 Norovirus infection
PLoS ONE
4
e5593
2009
Homo sapiens (Q10981)
brenda
Pettit, N.; Styslinger, T.; Mei, Z.; Han, W.; Zhao, G.; Wang, P.G.
Characterization of WbiQ: An alpha1->2-fucosyltransferase from Escherichia coli O127:K63(B8), and synthesis of H-type 3 blood group antigen
Biochem. Biophys. Res. Commun.
402
190-195
2010
Escherichia coli (Q5J7C6), Escherichia coli O127:K63(B8) (Q5J7C6)
brenda
Jasper, M.J.; Care, A.S.; Sullivan, B.; Ingman, W.V.; Aplin, J.D.; Robertson, S.A.
Macrophage-derived LIF and IL1B regulate alpha(1,2)fucosyltransferase 2 (Fut2) expression in mouse uterine epithelial cells during early pregnancy
Biol. Reprod.
84
179-188
2011
Mus musculus
brenda
Wu, Y.; Williams, M.; Bernard, S.; Driouich, A.; Showalter, A.; Faik, A.
Functional identification of two nonredundant Arabidopsis alpha(1,2)fucosyltransferases specific to arabinogalactan proteins
J. Biol. Chem.
285
13638-13645
2010
Arabidopsis thaliana
brenda
Tao, S.; He, Y.; Ying, Y.; Hong, X.; Xu, X.; Zhu, F.; Lv, H.; Yan, L.
C35T mutation could slightly decrease the activity of human alpha-(1,2)-fucosyltransferase
Transfus. Clin. Biol.
19
5-10
2012
Homo sapiens
brenda
Zeyland, J.; Wozniak, A.; Gawronska, B.; Juzwa, W.; Jura, J.; Nowak, A.; S?omski, R.; Smorag, Z.; Szalata, M.; Mazurek, U.; Lipinski, D.
Double transgenic pigs with combined expression of human alpha1,2-fucosyltransferase and alpha-galactosidase designed to avoid hyperacute xenograft rejection
Arch. Immunol. Ther. Exp.
62
411-422
2014
Homo sapiens (P19526)
brenda
Isozaki, T.; Ruth, J.H.; Amin, M.A.; Campbell, P.L.; Tsou, P.S.; Ha, C.M.; Haines, G.K.; Edhayan, G.; Koch, A.E.
Fucosyltransferase 1 mediates angiogenesis, cell adhesion and rheumatoid arthritis synovial tissue fibroblast proliferation
Arthritis Res. Ther.
16
R28
2014
Homo sapiens (P19526)
brenda
Gao, N.; Liu, J.; Liu, D.; Hao, Y.; Yan, L.; Ma, Y.; Zhuang, H.; Hu, Z.; Gao, J.; Yang, Z.; Shi, H.; Lin, B.
c-Jun transcriptionally regulates alpha 1, 2-fucosyltransferase 1 (FUT1) in ovarian cancer
Biochimie
107 Pt B
286-292
2014
Homo sapiens (P19526)
brenda
Engels, L.; Elling, L.
WbgL: A novel bacterial alpha1,2-fucosyltransferase for the synthesis of 2-fucosyllactose
Glycobiology
24
170-178
2014
Escherichia coli (A6M9C2), Escherichia coli O126 (A6M9C2)
brenda
Che, Y.; Ren, X.; Xu, L.; Ding, X.; Zhang, X.; Sun, X.
Critical involvement of the alpha(1,2)-fucosyltransferase in multidrug resistance of human chronic myeloid leukemia
Oncol. Rep.
35
3025-3033
2016
Homo sapiens (P19526)
brenda
Dicioccio, R.A.; Barlow, J.J.; Matta, K.L.
Modified procedure for detection of GDP-L-fucose:galactoside 2-fucosyltransferase
Clin. Chim. Acta
108
41-48
1980
Homo sapiens
brenda
Kyprianou, P.; Betteridge, A.; Donald, A.S.; Watkins, W.M.
Purification of the blood group H gene associated alpha-2-L-fucosyltransferase from human plasma
Glycoconj. J.
7
573-588
1990
Homo sapiens
brenda
Ohashi, H.; Ohashi, T.; Misaki, R.; Fujiyama, K.
Arabidopsis thaliana alpha1,2-l-fucosyltransferase catalyzes the transfer of l-galactose to xyloglucan oligosaccharides
FEBS Lett.
593
187-194
2019
Arabidopsis thaliana (Q9SWH5)
brenda
Chin, Y.W.; Kim, J.Y.; Kim, J.H.; Jung, S.M.; Seo, J.H.
Improved production of 2-fucosyllactose in engineered Escherichia coli by expressing putative alpha-1,2-fucosyltransferase, WcfB from Bacteroides fragilis
J. Biotechnol.
257
192-198
2017
Bacteroides fragilis
brenda
Bandini, G.; Damerow, S.; Sempaio Guther, M.L.; Guo, H.; Mehlert, A.; Paredes Franco, J.C.; Beverley, S.; Ferguson, M.A.
An essential, kinetoplastid-specific GDP-Fuc beta-D-Gal alpha-1,2-fucosyltransferase is located in the mitochondrion of Trypanosoma brucei
eLife
10
e70272
2021
Trypanosoma brucei brucei (Q38FH1), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q38FH1)
brenda
Zemkollari, M.; Ruprecht, C.; Blaukopf, M.; Grabherr, R.; Staudacher, E.
Cloning, expression and characterisation of a novel mollusc alpha-1,2-fucosyltransferase from Crassostrea gigas (CgFUT2)
Glycoconj. J.
41
255-265
2024
Magallana gigas
brenda
Li, M.; Zhang, T.; Li, C.; Gao, W.; Liu, Z.; Miao, M.
Semi-rationally designed site-saturation mutation of Helicobacter pylori alpha-1,2-fucosyltransferase for improved catalytic activity and thermostability
Int. J. Biol. Macromol.
259
129316
2024
Helicobacter pylori (WP_026938579.1), Helicobacter pylori ATCC 26695 (WP_026938579.1)
brenda
Zhu, Y.; Chen, R.; Wang, H.; Chen, Y.; Liu, Y.; Zhou, J.; Mu, W.
Elimination of byproduct generation and enhancement of 2-fucosyllactose synthesis by expressing a novel alpha1,2-fucosyltransferase in engineered Escherichia coli
J. Agric. Food Chem.
71
4915-4923
2023
Helicobacter sp. 11S02629-2
brenda
Shin, J.; Kim, S.; Park, W.; Jin, K.C.; Kim, S.K.; Kweon, D.H.
Directed evolution of soluble alpha-1,2-fucosyltransferase using kanamycin resistance protein as a phenotypic reporter for efficient production of 2-fucosyllactose
J. Microbiol. Biotechnol.
32
1471-1478
2022
Helicobacter pylori
brenda
Liu, W.; Tang, S.; Peng, J.; Zhu, Y.; Pan, L.; Wang, J.; Peng, X.; Cheng, H.; Chen, Z.; Wang, Y.; Zhou, H.
Enhancing lactose recognition of a key enzyme in 2-fucosyllactose synthesis alpha-1,2-fucosyltransferase
J. Sci. Food Agric.
103
1303-1314
2023
Helicobacter pylori
brenda
Paredes Franco, J.; Sampaio Guther, M.; Lima, M.; Ferguson, M.
Characterisation of TcFUT1, a mitochondrial fucosyltransferase from Trypanosoma cruzi
Mol. Biochem. Parasitol.
256
111590
2023
Trypanosoma cruzi
brenda
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