Any feedback?
Information on EC 2.4.1.152 - 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase and Organism(s) Helicobacter pylori and UniProt Accession O30511
for references in articles please use BRENDA:EC2.4.1.152Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.1.152 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferaseIUBMB Comments
Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. This enzyme fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4, unlike EC 2.4.1.65, 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase, which fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3.
Specify your search results
Word Map
- 2.4.1.152
-
sialylated
-
fucosylated
- selectins
- fuc-tiii
- n-acetyllactosamine
- medicine
- synthesis
-
alpha1,3-fucosylation
- lewisx
- fuc-ts
- fuct-iv
- alpha-2-l-fucosyltransferase
- analysis
- drug development
- biotechnology
The taxonomic range for the selected organisms is: Helicobacter pylori
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
fuc-tv, alpha-3-fucosyltransferase, fucosyltransferase 4, alpha-3-l-fucosyltransferase, alpha1,3 fuct-vii, fut vi, alpha1,3ft, alpha1,3-fuct, fucosyltransferase-vii, fucosyltransferase ix, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha(1-3)fucosyltransferase
-
-
-
-
alpha-3-fucosyltransferase
-
-
-
-
alpha-3-L-fucosyltransferase
-
-
-
-
alpha1,3 fucosyltransferase
alpha1,3FT
-
-
-
-
alpha1-3 fucosyltransferase
-
-
-
-
alpha1->3fucosyltransferase
-
-
-
-
alpha3-fucosyltransferase-V
-
-
-
-
alpha3-fucosyltransferase-VI
-
-
-
-
Fuc-Tb
-
-
-
-
Fuc-TV
-
-
-
-
fucosyltransferase, guanosine diphosphofucose-glucoside alpha1-->3-
-
-
-
-
FucT-VI
-
-
-
-
FUT5
-
-
-
-
FUT6
-
-
-
-
FutA
galactoside 3-fucosyltransferase
-
-
-
-
GDL-L-fucose:N-acetyl-beta-D-glucosaminyl alpha-3-L-fucosyltransferase
-
-
-
-
GDP-Fuc:Galbeta1-4GlcNAc (Fuc to GlcNAc) alpha1-3 fucosyltransferase
-
-
-
-
GDP-fucose:beta-D-N-acetylglucosaminide 3-alpha-fucosyltransferase
-
-
-
-
GDP-fucose:Galbeta(1-4)GlcNAc-R alpha(1-3)fucosyltransferase
-
-
-
-
GDP-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-galactosaminyl-R 3-L-fucosyltransferase
-
-
-
-
guanosine diphosphofucose glucoside alpha1->3fucosyltransferase
-
-
-
-
lewis-negative alpha-3-fucosyltransferase
-
-
-
-
plasma alpha-3-fucosyltransferase
-
-
-
-
alpha1,3 fucosyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R 3-alpha-L-fucosyltransferase (configuration-inverting)
Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. This enzyme fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4, unlike EC 2.4.1.65, 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase, which fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3.
CAS REGISTRY NUMBER
COMMENTARY
111310-38-4
-
39279-34-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-beta-fucose + lacto-N-neotetraose
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc
-
-
-
?
GDP-beta-fucose + lactose
GDP + alpha1,3-fucosyllactose
N-acetyllactosamine is preferred over lactose
-
-
?
GDP-beta-fucose + N-acetyllactosamine
GDP + alpha1,3-fucosyl-N-acetyllactosamine
N-acetyllactosamine is preferred over lactose. At a low GDP-fucose to acceptor ratio, the enzyme selectively fucosylates N-acetyllactosamine
-
-
?
GDP-6,7-dideoxy-beta-L-galacto-hept-6-enopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl 6,7-dideoxy-beta-L-galacto-hept-6-enopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
-
-
-
?
GDP-6-azido-6-deoxy-beta-L-galactopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl -6-azido-6-deoxy-beta-L-galactopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
-
-
-
?
GDP-6-deoxy-6-fluoro-beta-L-galactopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl -6-deoxy-6-fluoro-beta-L-galactopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
-
-
-
?
GDP-6-O-methyl-beta-L-galactopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl 6-O-methyl-beta-L-galactopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
-
-
-
?
GDP-alpha-D-(5-cyano)arabinopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl alpha-D-(5-cyano)arabinopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
-
-
-
?
GDP-alpha-D-arabinopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl alpha-D-arabinopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
-
-
-
?
GDP-beta-L-fucose + 4-deoxy-Galbeta1,4GlcNAc
?
-
8% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + D-lactose
GDP + 3 L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-Glc
-
the enzyme has very low relative substrate specificity toward D-lactose
-
-
?
GDP-beta-L-fucose + N-acetyl-D-lactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
-
-
-
-
?
GDP-beta-L-fucose + NeuAcalpha2,3Galbeta1,4GlcNAc
?
-
32% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-galactopyranose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl beta-L-galactopyranosyl-(1->3)-[beta-D-galactopyranosyl-(1->4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
-
-
-
?
GDP-L-fucose + 2-azidoethyl 2-(acetylamino)-2-deoxy-4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + 2-azidoethyl 6-deoxy-beta-L-galactopyranosyl-(1-3)-[beta-D-galactopyranosyl-(1-4)]-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
-
-
-
?
GDP-L-fucose + Galbeta(1,4)GlcNAc-O(CH2)8CO2CH3
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-O(CH2)8CO2CH3
-
-
-
-
?
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc
?
-
135% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc
?
-
72% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
-
115% of the activity with Galbeta1,4GlcNAc
-
-
?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
-
99% of the activity with Galbeta1,4GlcNAc
-
-
?
additional information
?
-
enzyme accepts fluorescein-isothiocyanate-labeled fucose and carboxyfluorescein-labeled fucose. Fluorescein-isothiocyanate-labeled NDP-beta-L-fucose is the best of these substrates
-
-
-
additional information
?
-
-
the enzyme shows alpha1,3- and alpha1,4-fucosyltransferase activity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.448
GDP-beta-fucose
cosubstrate N-acetyllactosamine, pH 7.5, 37°C
0.39
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1441)
1.7
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1428)
0.0156
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1441)
0.0176
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1428)
0.0447
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, full-length enzyme
0.056
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, full-length enzyme
0.24
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I, at pH 7.6 and 37°C
0.28
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/S46F, at pH 7.6 and 37°C
0.3
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.617
GDP-beta-fucose
cosubstrate N-acetyllactosamine, pH 7.5, 37°C
5.97
D-lactose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
1.1
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1428)
2.3
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
-
truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1428)
0.478
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I, at pH 7.6 and 37°C
1.1
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1428)
1.328
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/S46F, at pH 7.6 and 37°C
1.512
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
2.3
GDP-beta-L-fucose
-
cosubstrate: Galbeta1,4GlcNAc-O(CH2)8CO2CH3, truncated enzyme alpha-(1,3/1,4)-fucosyltransferase(1428)
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.096
GDP-beta-fucose
cosubstrate N-acetyllactosamine, pH 7.5, 37°C
0.083
D-lactose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
1.992
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I, at pH 7.6 and 37°C
4.742
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/S46F, at pH 7.6 and 37°C
5.041
GDP-beta-L-fucose
-
mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51200
51200
-
x * 51200, alpha-(1,3/1,4)-fucosyltransferase(1-428), calculated from sequence
51200
-
x * 51200, mutant alpha-(1,3/1,4)-fucosyltransferase (1441), calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 51200, alpha-(1,3/1,4)-fucosyltransferase(1-428), calculated from sequence
?
-
x * 51200, mutant alpha-(1,3/1,4)-fucosyltransferase (1441), calculated from sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A128N
A128N/H129E
-
the mutant displays 6.5fold higher catalytic activity with D-lactose than the wild type enzyme
additional information
A128N
-
the mutant displays 3.4fold higher catalytic activity with D-lactose than the wild type enzyme
A128N
mutant obtained by focused directed evolution mutant, 3.4fold higher catalytic activity than wild-type
additional information
-
with full length 11639FucT, 28% of total enzyme activities is localized in the soluble fraction. For alpha-(1,3/1,4)-fucosyltransferase(1441), this increases to 45%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. Truncation mutant alpha-(1,3/1,4)-fucosyltransferase(10447) completely loses activity
additional information
-
with full length UA948FucT, 20% of total enzyme activities is localized in the soluble fraction. For UA948(1-428), this increases to 47%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. UA948(1-364), a mutant with the entire heptad repeat region removed, exhibits extremely low levels of enzyme activity. This indicates that the heptad repeat region is essential for enzyme activity. Construct alpha-(1,3/1,4)-fucosyltransferase(1-371) has little enzyme activity. alpha-(1,3/1,4)-fucosyltransferase(10-434) and alpha-(1,3/1,4)-fucosyltransferase(1-434) completely lose activity
additional information
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
additional information
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
additional information
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
additional information
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
additional information
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
additional information
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
additional information
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
additional information
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
additional information
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilized alpha-(1,3/1,4)-fucosyltransferase(1-428) loses 23% of its activity after 3 month
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilized alpha-(1,3/1,4)-fucosyltransferase(1441) loses 38% activity after 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alpha-(1,3/1,4)-fucosyltransferase(1428) with a His6 tag at the C terminus is purified
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length and each truncated FucT (DELTAFucT) are expressed in Escherichia coli HMS174DE3
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
synthesis of fluorescein-isothiocyanate-labeled and carboxyfluorescein-labeled NDP-beta-L-fucose derivatives, and application in labeling of different glycoproteins with the aid of fucosyltransferases. The fluorescein-isothiocyanate-labeled fucose is the best of these substrates, and the bacterial enzyme FucT tolerates the fluorescent substrates better than human fucosyltransferases
synthesis
expression of bacterial alpha-1,3-fucosyltransferase in engineered Escherichia coli deficient in beta-galactosidase activity and expressing the essential enzymes for the production of guanosine 5'-diphosphate-L-fucose, for synthesis of 3-fucosyllactose. The fucT gene gives the best 3-fucosyllactose production in a simple batch fermentation process using glycerol as a carbon source and lactose as an acceptor. With concomitant blocking the colanic acid biosynthetic pathway, the recombinant strain exhibits the highest concentration (11.5 g/l), yield (0.39 mol/mol), and productivity (0.22 g/l/h) of 3-fucosyllactose in glycerol-limited fed-batch fermentation
synthesis
synthesis
a chemoenzymatic model for the preparative-scale synthesis of a diverse array of GDP-fucose derivatives is reported
synthesis
to overcome the poor solubility of FutA upon expression in Escherichia coli, codon optimization, and systematic truncation of the protein at the C-terminus with only one heptad repeat remaining yield 150-200 mg/l of soluble protein of FutA and result in more than an 18fold increase in the 3-fucosyllactose yield. Mutant A128N obtained by focused directed evolution mutant displays a 3.4fold higher catalytic activity than wild-type FutA. Mutant A128N/H129E/Y132I exhibits a 9.6fold improvement in specific activity when compared to wild-type. Mutants A128N/H129E/S46F and A128N/H129E/Y132I/S46F show synergistic effects, that is 14.5- and 15.5fold improvement in specific activity relative to wild-type. The mutations increase the binding affinity for lactose and kcat values for lactose and GDP-fucose. The quadruple mutant A128N/H129E/Y132I/S46F synthesizes 3-fucosyllactose with an improved yield and productivity (more than 96% yield based on 5 mM of GDP-Fuc within 1 h)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ma, B.; Audette, G.F.; Lin, S.; Palcic, M.M.; Hazes, B.; Taylor, D.E.
Purification, kinetic characterization, and mapping of the minimal catalytic domain and the key polar goups of Helicobacter pylori alpha-(1,3/1,4)-fucosyltransferases
J. Biol. Chem.
281
6385-6394
2006
Helicobacter pylori, Helicobacter pylori NCTC11639, Helicobacter pylori UA948
Wang, W.; Hu, T.; Frantom, P.A.; Zheng, T.; Gerwe, B.; Del Amo, D.S.; Garret, S.; Seidel, R.D.; Wu, P.
Chemoenzymatic synthesis of GDP-L-fucose and the Lewis X glycan derivatives
Proc. Natl. Acad. Sci. USA
106
16096-16101
2009
Helicobacter pylori (O25366)
Choi, Y.H.; Kim, J.H.; Park, B.S.; Kim, B.G.
Solubilization and iterative saturation mutagenesis of alpha1,3-fucosyltransferase from Helicobacter pylori to enhance its catalytic efficiency
Biotechnol. Bioeng.
113
1666-1675
2016
Helicobacter pylori
Choi, Y.H.; Kim, J.H.; Park, B.S.; Kim, B.G.
Solubilization and Iterative Saturation Mutagenesis of alpha1,3-fucosyltransferase from Helicobacter pylori to enhance its catalytic efficiency
Biotechnol. Bioeng.
113
1666-1675
2016
Helicobacter pylori (O25142), Helicobacter pylori 26695 (O25142)
Jung, S.; Park, Y.; Seo, J.
Production of 3-fucosyllactose in engineered Escherichia coli with alpha-1,3-fucosyltransferase from Helicobacter pylori
Biotechnol. J.
14
1800498
2019
Helicobacter pylori (O30511)
Bai, J.; Wu, Z.; Sugiarto, G.; Gadi, M.R.; Yu, H.; Li, Y.; Xiao, C.; Ngo, A.; Zhao, B.; Chen, X.; Guan, W.
Biochemical characterization of Helicobacter pylori alpha1-3-fucosyltransferase and its application in the synthesis of fucosylated human milk oligosaccharides
Carbohydr. Res.
480
1-6
2019
Helicobacter pylori (O30511)
Seelhorst, K.; Pahnke, K.; Meier, C.; Hahn, U.
Tagging glycoproteins with fluorescently labeled GDP-fucoses by Using alpha1,3-fucosyltransferases
ChemBioChem
16
1919-1924
2015
Helicobacter pylori (O30511), Homo sapiens (Q11130), Homo sapiens (Q9Y231)
Yu, J.; Shin, J.; Park, M.; Seydametova, E.; Jung, S.M.; Seo, J.H.; Kweon, D.H.
Engineering of alpha-1,3-fucosyltransferases for production of 3-fucosyllactose in Escherichia coli
Metab. Eng.
48
269-278
2018
Helicobacter pylori (J0U361), Helicobacter pylori (O25142), Helicobacter pylori (O25366), Helicobacter pylori ATCC 43504 (J0U361), Helicobacter pylori ATCC 700392 (O25142), Helicobacter pylori ATCC 700392 (O25366)
EXTERNAL LINKS (specific for EC-Number 2.4.1.152)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
