Information on EC 2.4.1.214 - glycoprotein 3-alpha-L-fucosyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.4.1.214
-
RECOMMENDED NAME
GeneOntology No.
glycoprotein 3-alpha-L-fucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GDP-beta-L-fucose + N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}asparagine = GDP + N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl}asparagine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Various types of N-glycan biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-gluco
Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-alpha-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-beta-L-fucose to form an alpha1,3-linkage rather than an alpha1,6-linkage. The {iupac/misc/glycp#3.5::N-glycan} products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).
CAS REGISTRY NUMBER
COMMENTARY hide
68247-53-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
strain NCTC11639
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Schistosoma sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
suppression of isoform Fut10 expression induces the differentiation of neural stem cells and embryonic stem cells. In addition, enzyme knockdown in the cortical ventricular zone of the embryonic brain impairs the radial migration of neural precursor cells
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-alpha-L-fucose + fetuin
GDP + 3-alpha-L-fucosyl-fetuin
show the reaction diagram
-
-
-
-
?
GDP-alpha-L-fucose + Galbeta1-4GlcNAc-R
GDP + Galbeta1-4[Fucalpha1-3]GlcNAc-R
show the reaction diagram
-
-
-
-
ir
GDP-alpha-L-fucose + NeuAcalpha2-3Galbeta1-3GlcNAcbeta-R
GDP + NeuAcalpha2-3Galbeta1-3[Fucalpha1-3]GlcNAcbeta-R
show the reaction diagram
-
4% of the activity with NeuAcalpha2-3Galbeta1-4GlcNAc-R
-
-
?
GDP-alpha-L-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc
GDP + NeuAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAc
show the reaction diagram
-
28% of the activity with NeuAcalpha2-3Galbeta1-4GlcNAc-R
-
-
?
GDP-alpha-L-fucose + NeuAcalpha2-3Galbeta1-4GlcNAcbeta-R
GDP + NeuAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAcbeta-R
show the reaction diagram
-
best substrate
-
-
?
GDP-beta-fucose + fetuin
GDP + fucosylated fetuin
show the reaction diagram
-
-
-
-
?
GDP-beta-L-fucose + (1->4)-beta-D-galactosyl-N-acetyl-D-glucosaminyl-L-Asn
GDP + (1->4)-beta-D-galactosyl-[alpha-(1->3)-L-fucosyl]-N-acetyl-D-glucosaminyl-L-Asn
show the reaction diagram
-
-
-
-
?
GDP-beta-L-fucose + GlcNAcbeta(1->2)Manalpha(1->6)(GlcNAcbeta(1-2)Manalpha(1->3))Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc
GDP + GlcNAcbeta(1->2)Manalpha(1->6)(GlcNAcbeta(1->2)Manalpha(1->3))Manbeta(1->4)GlcNAcbeta(1->4)(Fucalpha(1->3))GlcNAc
show the reaction diagram
-
-
-
?
GDP-beta-L-fucose + GlcNAcbeta(1->2)Manalpha(1->6)[GlcNAcbeta(1->2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc
GDP + GlcNAcbeta(1->2)Manalpha(1->6)[GlcNAcbeta(1->2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)[L-Fucalpha(1->3)]GlcNAc
show the reaction diagram
-
-
-
-
?
GDP-beta-L-fucose + GlcNAcbeta(1->2)Manalpha(1->6)[GlcNAcbeta(1->2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)[L-Fucalpha(1->6)]GlcNAc
GDP + GlcNAcbeta(1->2)Manalpha(1->6)[GlcNAcbeta(1->2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)[L-Fucalpha(1->3)][L-Fucalpha(1->6)]GlcNAc
show the reaction diagram
GDP-beta-L-fucose + Manalpha(1->6)(Manalpha(1->3))Manalpha(1->6)(Manalpha(1->3))Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc
GDP + Manalpha(1->6)(Manalpha(1->3))Manalpha(1->6)(Manalpha(1->3))Manbeta(1->4)GlcNAcbeta(1->4)[Fucalpha(1->3)]GlcNAc
show the reaction diagram
-
-
-
?
GDP-beta-L-fucose + Manalpha(1->6)[Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)[L-Fucalpha(1->6)]GlcNAc
GDP + Manalpha(1->6)[Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)[L-Fucalpha(1->3)][L-Fucalpha(1->6)]GlcNAc
show the reaction diagram
-
-
-
?
GDP-fucose + alpha1-acid glycoprotein
GDP + alpha1-3 fucosylated glycoprotein
show the reaction diagram
-
the activity of the LEC11 cells enzyme is considerably higher than the activity of the LEC12 cells enzyme
-
?
GDP-fucose + asialo-alpha1-acid glycoprotein
GDP + alpha1-3 fucosylated glycoprotein
show the reaction diagram
-
-
-
?
GDP-fucose + asialo/agalacto-glycopeptide-F2
GDP + alpha1-3-fucosylated glycopeptide
show the reaction diagram
-
asialo/agalacto-glycopeptide-F2: from human fibrinogen
-
?
GDP-fucose + asialo/agalacto-glycopeptide-IgGF6
GDP + alpha1-3-fucosylated glycopeptide
show the reaction diagram
-
asialo/agalacto-glycopeptide-IgGF6: from core alpha1-6-fucosylated human IgG
-
?
GDP-fucose + asialofetuin
GDP + alpha1-3 fucosylated glycoprotein
show the reaction diagram
-
-
-
?
GDP-fucose + asialotransferrin
GDP + alpha1-3 fucosylated glycoprotein
show the reaction diagram
-
-
-
?
GDP-fucose + bisected agalacto-glycopeptide-IgGF6
GDP + alpha1-3-fucosylated glycopeptide
show the reaction diagram
-
-
-
?
GDP-fucose + dabsyl-GnGn-peptide
GDP + alpha1-3-fucosylated dabsyl-GnGn-peptide
show the reaction diagram
GDP-fucose + dabsylated-GalGal-peptide
GDP + alpha1-3-fucosylated peptide
show the reaction diagram
-
0.7% relative activity with recombinant enzyme
-
?
GDP-fucose + dabsylated-GalGn-peptide
GDP + alpha1-3-fucosylated peptide
show the reaction diagram
-
50% relative activity with recombinant enzyme
-
?
GDP-fucose + dansyl-GnGn
GDP + alpha1-3-fucosylated glycopeptide
show the reaction diagram
GDP-fucose + dansyl-GnGnF6
GDP + alpha1-3-fucosylated glycopeptide
show the reaction diagram
-
prefucosylation of GnGn with chicken heart extract results in a superior conversion of GnGnF6 by FucTA than with GnGn, 100% relative conversion
-
?
GDP-fucose + dansylated mono-beta1,3-galactosylated glycopeptide
GDP + alpha1-3-fucosylated glycopeptide
show the reaction diagram
-
FucTA gene
-
?
GDP-fucose + fetuin
GDP + alpha1-3 fucosylated glycoprotein
show the reaction diagram
-
the activity of the LEC11 cells enzyme is considerably higher than the activity of the LEC12 cells enzyme
-
?
GDP-fucose + Galbeta1-4GlcNAcalpha-p-nitrophenol
Galbeta1-4(Fucalpha1-3)GlcNAcalpha-p-nitrophenol
show the reaction diagram
-
CFET-3 required no cations, CFET-4 required divalent cations
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-
-
GDP-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
show the reaction diagram
-
CFET-3 required no cations, CFET-4 required divalent cations
-
-
?
GDP-fucose + GalGal-N-glycan
GDP + alpha1-3-fucosylated GalGal-N-glycan
show the reaction diagram
-
4.6% relative conversion, FucTA gene
-
?
GDP-fucose + GalGalF6-N-glycan
GDP + alpha1-3-fucosylated GalGalF6-N-glycan
show the reaction diagram
-
19.8% relative conversion, FucTA gene
-
?
GDP-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
show the reaction diagram
-
LDNT, CFET-2
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-
-
GDP-fucose + GlcNAcbeta1-2-Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)GlcNAcbeta1-Asn
GDP + GlcNAcbeta1-2-Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)(Fucalpha1-3)GlcNAcbeta1-Asn
show the reaction diagram
-
-
-
?
GDP-fucose + GlcNAcbeta1-2-Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAcbeta1-Asn
GDP + GlcNAcbeta1-2-Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-Asn
show the reaction diagram
-
-
-
?
GDP-fucose + GlcNAcbeta1-2-Manalpha1-3[Manalpha1-3(Manalpha1-6)Manalpha1-6]Manbeta1-4-GlcNAcbeta1-4GlcNAcbeta1-Asn
GDP + GlcNAcbeta1-2-Manalpha1-3[Manalpha1-3(Manalpha1-6)Manalpha1-6]Manbeta1-4-GlcNAcbeta1-4 (Fucalpha1-3)GlcNAcbeta1-Asn
show the reaction diagram
-
-
-
?
GDP-fucose + GlcNAcbeta1-2-Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)GlcNAcbeta1-N-Asn-peptide(Nac)
GDP + GlcNAcbeta1-2-Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)(Fucalpha1-3)GlcNAcbeta1-N-Asn-peptide(Nac)
show the reaction diagram
-
-
the product shows a difucosylated structure with two Fuc residues at the Asn-bound GlcNAc residue, 40% yield
?
GDP-fucose + GlcNAcbeta1-2Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4(Fucalpha1-6)GlcNAcbeta1-Asn
GDP + GlcNAcbeta1-2Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-3)[Fucalpha1-6]GlcNAcbeta1-Asn
show the reaction diagram
-
difucosylated glycan structure
-
?
GDP-fucose + GlcNAcbeta1-2Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-Asn
GDP + GlcNAcbeta1-2Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4(Fucalpha1-3)GlcNAcbeta1-Asn
show the reaction diagram
-
-
-
?
GDP-fucose + GnGn + F(Ac)
GDP + alpha1-3-fucosylated peptide
show the reaction diagram
-
-
-
?
GDP-fucose + GnGn-oligosaccharide
GDP + alpha1-3 fucosylated GnGn-oligosaccharide
show the reaction diagram
-
93% relative activity of pure enzyme
-
?
GDP-fucose + GnGn-peptide
GDP + alpha1-3 fucosylated peptide
show the reaction diagram
-
100% relative activity of pure enzyme and of crude extract
-
?
GDP-fucose + GnGn-peptide
GDP + alpha1-3-fucosylated peptide
show the reaction diagram
-
100% relative activity with recombinant enzyme
-
?
GDP-fucose + GnGnF6-oligosaccharide
GDP + alpha1-3 fucosylated oligosaccharide
show the reaction diagram
-
95% relative activity of pure enzyme
-
?
GDP-fucose + GnGnF6-peptide
GDP + alpha1-3-fucosylated GnGnF6-peptide
show the reaction diagram
GDP-fucose + M5Gn-Asn
GDP + alpha1-3-fucosylated M5Gn-Asn
show the reaction diagram
-
71% relative activity with recombinant enzyme
-
?
GDP-fucose + Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)GlcNAcbeta1-Asn
Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)(Fucalpha1-3)GlcNAcb1-Asn
show the reaction diagram
-
CFET-1
-
-
?
GDP-fucose + Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAcbeta1-Asn
GDP + Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-Asn
show the reaction diagram
-
CFET-1, Nglycan pentasaccharide core acceptor as substrate
-
-
?
GDP-fucose + N-acetyllactosamine
GDP + alpha-1,3-fucosyl-N-acetyllactosamine
show the reaction diagram
-
-
-
?
GDP-fucose + N-acetyllactosamine
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc
show the reaction diagram
GDP-fucose + transferrin
GDP + alpha1-3 fucosylated glycoprotein
show the reaction diagram
-
-
-
?
GDP-L-fucose + GlcNAcbeta1,2Manalpha1,6(GlcNAcbeta1,2Manalpha1,3)Manbeta1,4GlcNAcbeta1,4(Fucalpha1,6)GlcNAc
GDP + GlcNAcbeta1,2Manalpha1,6(GlcNAcbeta1,2Manalpha1,3)Manbeta1,4GlcNAcbeta1,4(Fucalpha1,3)(Fucalpha1,6)GlcNAc
show the reaction diagram
-
preferred substrate
-
-
?
GDP-L-fucose + GlcNAcbeta1,2Manalpha1,6(GlcNAcbeta1,2Manalpha1,3)Manbeta1,4GlcNAcbeta1,4GlcNAc
GDP + GlcNAcbeta1,2Manalpha1,6(GlcNAcbeta1,2Manalpha1,3)Manbeta1,4GlcNAcbeta1,4(Fucalpha1,3)GlcNAc
show the reaction diagram
GDP-L-fucose + LacNAc-C8
GDP + alpha1,3-fucosylated LacNAc-C8
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-N-acetyl-beta-D-glucosaminyl]asparagine
GDP + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-[alpha-L-fucosyl-(1-3)]-N-acetyl-beta-D-glucosaminyl]asparagine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GDP-alpha-L-fucose + Galbeta1-4GlcNAc-R
GDP + Galbeta1-4[Fucalpha1-3]GlcNAc-R
show the reaction diagram
-
-
-
-
ir
GDP-beta-L-fucose + GlcNAcbeta(1->2)Manalpha(1->6)(GlcNAcbeta(1-2)Manalpha(1->3))Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc
GDP + GlcNAcbeta(1->2)Manalpha(1->6)(GlcNAcbeta(1->2)Manalpha(1->3))Manbeta(1->4)GlcNAcbeta(1->4)(Fucalpha(1->3))GlcNAc
show the reaction diagram
Q9C8W3
-
-
-
?
GDP-beta-L-fucose + Manalpha(1->6)[Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)[L-Fucalpha(1->6)]GlcNAc
GDP + Manalpha(1->6)[Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)[L-Fucalpha(1->3)][L-Fucalpha(1->6)]GlcNAc
show the reaction diagram
G5EDR5
-
-
-
?
GDP-L-fucose + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-N-acetyl-beta-D-glucosaminyl]asparagine
GDP + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-[alpha-L-fucosyl-(1-3)]-N-acetyl-beta-D-glucosaminyl]asparagine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
inhibitory for CFET-1, 2, 3 and 4
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
slight inhibition at 3-5 mM
Ca2+
about 45% residual activity at 10 mM; about 75% residual activity at 10 mM
CDP
-
slight inhibition at 3-5 mM
Co2+
about 30% residual activity at 10 mM; about 35% residual activity at 10 mM
Fe2+
-
-
GDP-hexylamine
-
-
GDP-N-(biphenyl-4-ylmethyl)-5-(1H-1,2,3-triazol-1-yl)pentanamide
-
-
GDP-propylamine
-
-
GTP
-
strong inhibition
iodoacetamide
-
-
Mg2+
about 45% residual activity at 10 mM; about 70% residual activity at 10 mM
Mn2+
-
at concentrations above 40 mM
N-ethylmaleimide
NaCl
-
50% inhibition at 250 mM, complete inhibition at 500 mM and above
Ni2+
about 38% residual activity at 10 mM; about 5% residual activity at 10 mM
p-chloromercuribenzoate
-
at 0.05 mM: almost 30% of the original enzyme activity remains
panosialin K
-
specific inhibition of FucT-VII
-
Triton X-100
-
at concentrations above 0.5%
UDP
-
slight inhibition at 3-5 mM
additional information
-
no inhibition of the recombinant soluble enzyme by NEM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triton X-100
-
0.1-0.5% slightly enhances activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.49
bisected agalacto-glycopeptide-IgGF6
-
-
-
0.046 - 0.067
dansyl-GnGn
0.011
dansyl-GnGnF6
-
glycopeptide derived from IgG, FucTA gene
0.5
fetuin
-
recombinant soluble enzyme
-
0.0062
GDP-alpha-L-fucose
-
recombinant soluble enzyme
0.1 - 1
GDP-beta-L-fucose
0.065 - 1
GDP-fucose
0.019 - 0.336
GDP-L-fucose
0.42
GlcNAcbeta(1->2)Manalpha(1->6)[GlcNAcbeta(1->2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc
-
at 25°C, pH not specified in the publication
1
GlcNAcbeta(1->2)Manalpha(1->6)[GlcNAcbeta(1->2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)[L-Fucalpha(1->6)]GlcNAc
-
at 25°C, pH not specified in the publication
0.19 - 6.7
GnGn-peptide
0.06 - 0.13
GnGnF6-peptide
0.7 - 8.92
LacNAc
0.13 - 1.6
LacNAc-C8
0.23
M5Gn-Asn
-
-
0.71 - 12.77
N-acetyllactosamine
5.6
NeuAcalpha2-3Galbeta1-4GlcNAc
-
recombinant soluble enzyme
additional information
additional information
-
kinetics of wild-type and alpha 1,3 FucT motif mutants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
GlcNAcbeta(1->2)Manalpha(1->6)[GlcNAcbeta(1->2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc
Apis mellifera
-
at 25°C, pH not specified in the publication
89214
0.097
GlcNAcbeta(1->2)Manalpha(1->6)[GlcNAcbeta(1->2)Manalpha(1->3)]Manbeta(1->4)GlcNAcbeta(1->4)[L-Fucalpha(1->6)]GlcNAc
Apis mellifera
-
at 25°C, pH not specified in the publication
89213
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00059
GDP-N-(biphenyl-4-ylmethyl)-5-(1H-1,2,3-triazol-1-yl)pentanamide
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000001
-
LEC12 mutant, substrate: alpha1-acid glycoprotein
0.000002
-
LEC11 mutant with transferrin as substrate and LEC12 mutant with fetuin as substrate
0.000003
-
LEC12 mutant, substrate: transferrin
0.000007
-
LEC11 mutant, substrate: asialotransferrin
0.000013
-
LEC11 mutant, substrate: asialofetuin
0.000014
-
LEC11 mutant with fetuin as substrate and LEC12 mutant with asialofetuin as substrate
0.000015
-
LEC11 mutant, substrate: alpha1-acid glycoprotein
0.000016
-
LEC12 mutant, substrate: asialo-alpha1-acid glycoprotein or asialotransferrin
0.000019
-
LEC11 mutant, substrate: asialo-alpha1-acid glycoprotein
0.071
-
-
0.38
deletion mutant FTdelta115 with 115 residues deleted from the C-terminus, substrate LacNAc
1.6
-
purified recombinant soluble enzyme
2.52
deletion mutant FTdelta23 with 23 residues deleted from the C-terminus, substrate LacNAc
4.84
deletion mutant FTdelta28 with 28 residues deleted from the C-terminus, substrate LacNAc
5.04
deletion mutant FTdelta38 with 38 residues deleted from the C-terminus, substrate LacNAc
5.2
deletion mutant FTdelta80 with 80 residues deleted from the C-terminus, substrate LacNAc
5.72
deletion mutant FTdelta45 with 45 residues deleted from the C-terminus, substrate LacNAc
5.82
deletion mutant FTdelta66 with 66 residues deleted from the C-terminus, substrate LacNAc
43.35
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
-
-
7 - 10
-
the recombinant enzyme shows a broad pH-optimum
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
more than 50% activity between pH 5.0 and 7.0
6 - 11
-
enzyme is not affected by high pH but shows no activity at pH below pH 5.5
6.5 - 8
more than 50% activity between pH 6.5 and 8.0
7.5 - 9
enzyme shows maximal activity in mildly alkaline conditions
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
glycosyltransferase assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
more than 50% activity between 10 and 40°C; more than 50% activity between 10 and 40°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
mechanism of FucT-VII induction, overview
Manually annotated by BRENDA team
-
glycosylation mutants LEC11 and LEC12
Manually annotated by BRENDA team
-
high enzyme expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
lumenal side of the membrane
Manually annotated by BRENDA team
additional information
-
in the cytoplasm of mock transfectant
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
x * 45000, SDS-PAGE
46000
x * 46000, SDS-PAGE
51000
-
SDS-PAGE, Western blot
53000
calculation from sequence of cDNA
54000
-
x * 54000, major isoform, SDS-PAGE
56000
-
x * 56000, represents the same enzyme as the band with 54kDA, SDS-PAGE
56210
-
FucTA gene, amino acid sequence analysis
56700
-
x * 56700, FLAG-tagged enzyme, SDS-PAGE
61000
x * 61000, SDS-PAGE
64000
-
gel filtration
65000
-
1 * 65000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 65000, SDS-PAGE
additional information
-
6 neighboring cysteine residues in the enzyme, Cys68-Cys76 at the N-terminus, Cys211-Cys214 in the middle, and Cys318-Cys321 at the C-terminus, are engaged in disulfide bridges, forming small loop structures, enzyme structure modeling using sequnce analysis, mass spectrometry, fold recognition and homology modeling
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by the hanging drop vapor diffusion method, as FucT, FucT-GDPfucose and FucT-GDP complexes
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23 - 37
-
loss of activity at 37°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by chromatography on DE52 cellulose and Affigel Blue, chromatofocusing using PBE 94 and polybuffer 96, gelfiltration on a Sephacryl S200 column and affinity chromatography on a GnGn-column
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography and Affi-Gel Blue Sepharose column chromatography; Ni-NTA column chromatography and Affi-Gel Blue Sepharose column chromatography
Ni-NTA or HisTrap column chromatography
of Fuc-T C3, using Triton X-100 extraction and column chromatography on DE52 cellulose, Affi-Gel blue, S-Sepharose, GnGn-Sepharose and GDP-hexanolamine-Sepharose
-
recombinant soluble enzyme from CHO cells by GDP-hexanolamine affinity chromatography to homogeneity
-
recombinant soluble protein A-fusion wild-type and mutant FucT VIs from COS-7 cells by IgG affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1121-bp PCR product of cDNA containing the full length of the FUT7 gene ligated into the pM.D.18-T cloning vector, propagation in Escherichia coli DH5alpha. Full coding sequence of FUT7 subcloned into pIRES2-EGFP expression vector and transiently transfected into RL95-2 cells or injected into the uteri of early pregnant mice
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cDNA cloning of Fuc-T C3 from mRNA, recombinant enzyme expressed in Sf21 insect cells using baculovirus vector
-
expressed in Pichia pastoris
-
expressed in Pichia pastoris GS115 cells; expressed in Pichia pastoris GS115 cells
expressed in Pichia pastoris strain GS115
expressed in Spodoptera frugiperda Sf9 cells
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expression in CHO cells
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expression in COS7 cells, fusion of CFET-1 to green fluorescent protein
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expression in Escherichia coli DH5alpha or BL21
expression in Pichia pastoris GS115 cells; expression in Sf9 cells; the Apis mellifera genome encodes three alpha1,3-FucT homologues FucTA, FucTB and FucTC, expressed in yeast and insect cells only FucTA is found to be a core alpha1,3-FucT (EC 2.1.214), FucTC discloses to be the first Lewis-type alpha1,3-FucT (EC 2.4.1.152) to be described in insects, FucTB does not show any activity
expression of FucT-VII in H7721 hepatocarcinoma cells
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expression of the soluble enzyme, by constructing a fusion enzyme amino acid residues 1-63 of a mammalian enzyme fused to the stem and the catalytic region of residues 39-342 of the enzyme, in CHO cells
-
expression of wild-type and mutant FucT VIs in COS-7 cells as soluble N-terminal protein A-fusion proteins, mutant K241A shows a low expression level
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expression of wild-type enzyme, in Pichia pastoris strain GS115
-
FucT cDNA (414 bp) amplified and cloned into the BamHI site of puc18XTI2 to create puc18Fsi. The antisense fragment amplified and cloned into the KpnI digested vector puc18Fsi to generate puc18Fsias. Subsequently, the 'sense-intron-antisense' cassette excised by XbaI digestion and cloned into XbaI linearized plant expression vector pGA643
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gene FUT7, stable expression in MOLT-4 8H cells being induced by the recombinant enzyme in presence of mifepristone to produce sL2x epitopes, expression of Staphylococcus aureus protein A-human FucT-VII fusion protein in Spodoptera frugiperda Sf21 insect cells via the baculovirus infection system
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overexpression Escherichia coli to obtain a selenomethionine-labeled L202M FucT for crystallization
-
the complex of the FUT7-cytoplasmic tail and bovine UDP-galactose:beta-N-acetylglucosaminide: beta1,4-galactosyltransferase 1 is expressed in Sf9 insect cells
-
three genes FucTA, FucTB and FucTC encode proteins similar to alpha1-3-fucosyltransferases, expression in Pichia pastoris
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of FUT7 and sLeX is significantly increased after transfection of pIRES2-EGFP-FUT7 into RL95-2 cells compared with the parental control and mock vector transfectants
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RNAi-targeted down-regulation of the endogenous FucT
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N219A
the mutant retains 1.2% of the wild type activity
N337A
the mutant retains 18.6% of the wild type activity
R226A
the mutation leads to a complete loss of activity
S218A
the mutation completely abolishes the enzyme activity
S253A
the mutant retains 35.6% of the wild type activity
S483A
the mutant retains 32.2% of the wild type activity
T339A
the mutant retains 12.1% of the wild type activity
T422A
the mutant retains 36.5% of the wild type activity
Y243A
the mutant retains 9.8% of the wild type activity
D303E
the mutant retains 23.8% of the wild type activity
N194Q
glycosylation site mutant with less than 1% of wild type activity
S243A
the mutant retains 16.2% of the wild type activity
T361A
the mutant retains 24.3% of the wild type activity
E249A
-
FucT 45, no activity
E249D
-
FucT 45, no activity
E249Q
-
FucT 45, no activity
E95A
-
FucT 45, no activity
E95D
-
FucT 45, no activity
K250A
-
FucT 45, no activity
L202M
-
to introduce methionine
N240D
-
FucT 45, active
R195A
-
FucT 45, no activity
R195K
-
FucT 45, active
Y246A
-
FucT 45, active
Y246F
-
FucT 45, active
E249A
-
FucT 45, no activity
-
E249D
-
FucT 45, no activity
-
E249Q
-
FucT 45, no activity
-
K250A
-
FucT 45, no activity
-
Y246A
-
FucT 45, active
-
E247A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
E257A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
F242A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
F246A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, 7% activity compared to the wild-type FucT VI
K241A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, low expression level in COS-7 cells, below 1% activity compared to the wild-type FucT VI
K258A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, inactive mutant
L244A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, 7% activity compared to the wild-type FucT VI
N248A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
S249A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, 57% activity compared to the wild-type FucT VI
T256A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
Y240A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, 14% activity compared to the wild-type FucT VI
Y254A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, inactive mutant
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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RNA interference technology obtains a targeted down-regulation of the endogenous beta1,2-xylosyltransferase (XylT) and alpha1,3-fucosyltransferase (FucT) genes, whereby generating RNAi lines which are stable, viable and do not show any obvious phenotype, thus providing a robust tool for the production of therapeutically relevant glycoproteins in plants with a humanized N -glycan structure
pharmacology
-
the enzyme is a target for rational inhibitor design for medication in the treatment of rheumatoid arthritis
Show AA Sequence (226 entries)
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