Information on EC 2.4.1.152 - 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase

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

EC NUMBER
COMMENTARY hide
2.4.1.152
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RECOMMENDED NAME
GeneOntology No.
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GDP-beta-L-fucose + (1->4)-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R = GDP + (1->4)-beta-D-galactosyl-[alpha-(1->3)-L-fucosyl]-N-acetyl-D-glucosaminyl-R
show the reaction diagram
i.e. Lewis X determinent
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ABH and Lewis epitopes biosynthesis from type 2 precursor disaccharide
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biosynthesis of Lewis epitopes (H. pylori)
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Glycosphingolipid biosynthesis - globo and isoglobo series
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Glycosphingolipid biosynthesis - lacto and neolacto series
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Mannose type O-glycan biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:(1->4)-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-alpha-L-fucosyltransferase
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 hide
111310-38-4
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39279-34-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
strain NCTC11639
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Manually annotated by BRENDA team
strain UA948
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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suppression of isoform Fut10 expression induces the differentiation of neural stem cells and embryonic stem cells. In addition, knockdown of Fut10 expression in the cortical ventricular zone of the embryonic brain impairs the radial migration of neural precursor cells
metabolism
the enzyme is specifically responsible for Sialyl-Lewis X synthesis
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
6-deoxy-6-N-(2-naphthalene-2-yl-acetamide)-beta-L-galactopyranos-1-yl-guanosine 5'-diphosphate + sialyl-alpha-2,3-LacNAc-O-(CH2)3-N-dansyl
GDP + Galbeta(1-4)-[6-deoxy-6-N-(2-naphthalene-2-yl-acetamide)-L-Galbeta(1-3)]GlcNAc-O-(CH2)3-N-dansyl
show the reaction diagram
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via intermediate 6-azid0-1,2,3,4-tetra-O-benzoyl-6-deoxy-beta-L-galactopyranose, 6-deoxy-6-N-(2-naphalene-2-yl-acetamide)-beta-L-galactopyranos-1-yl-guanosine 5'-diphosphate disodium salt is the most sensitive and selective donor substrate for FUT-VI among all of the GDP-Fuc analogues, including the parent GDP-Fuc, known to date
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?
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
show the reaction diagram
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-
-
?
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
show the reaction diagram
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-
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?
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
show the reaction diagram
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-
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?
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
show the reaction diagram
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-
-
?
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
show the reaction diagram
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-
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?
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
show the reaction diagram
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?
GDP-beta-fucose + alpha2,3-sialyl N-acetyllactosamine
GDP + alpha1,3-fucosyl-alpha2,3-sialyl-N-acetyllactosamine
show the reaction diagram
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FucT-VII and FucT-IV
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?
GDP-beta-fucose + alpha2,3-sialyl N-acetyllactosaminyl-R
GDP + alpha1,3-fucosyl-alpha2,3-sialyl-N-acetyllactosaminyl-R
show the reaction diagram
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FucT-VII and FucT-IV
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?
GDP-beta-fucose + N-acetyllactosamine
GDP + alpha1,3-fucosyl-N-acetyllactosamine
show the reaction diagram
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FucT-VI
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?
GDP-beta-L-fucose + 3-sulfo-Galbeta1,4GlcNAc
?
show the reaction diagram
GDP-beta-L-fucose + 4-deoxy-Galbeta1,4GlcNAc
?
show the reaction diagram
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8% of the activity with Galbeta1,4GlcNAc
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?
GDP-beta-L-fucose + asialo-erythropoietin
?
show the reaction diagram
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wild-type FUT9 efficiently fucosylates di-, tri- and tetraantennary N-glycans from asialoEPO
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?
GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R
GDP + beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-R
show the reaction diagram
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?
GDP-beta-L-fucose + D-lactose
GDP + 3 L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-Glc
show the reaction diagram
GDP-beta-L-fucose + fetuin
?
show the reaction diagram
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?
GDP-beta-L-fucose + fetuin-biotin
?
show the reaction diagram
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?
GDP-beta-L-fucose + Fucalpha1,2Galbeta1,4GlcNAc
?
show the reaction diagram
GDP-beta-L-fucose + Galbeta1,4GlcNAc
?
show the reaction diagram
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?
GDP-beta-L-fucose + Galbeta1-4GlcNAcalpha-4-nitrophenol
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcalpha-4-nitrophenol
show the reaction diagram
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preferred substrate of CEFT-4 and CEFT-3
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?
GDP-beta-L-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
show the reaction diagram
GDP-beta-L-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc
show the reaction diagram
GDP-beta-L-fucose + N-acetyl-D-lactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
show the reaction diagram
GDP-beta-L-fucose + N-acetyllactosamine
GDP + ?
show the reaction diagram
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?
GDP-beta-L-fucose + N-acetyllactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
show the reaction diagram
GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-6-O-sulfo-GlcNAc beta-O-C3H6-biotin
?
show the reaction diagram
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i.e. 6-sulfo-3'SLN, best substrate
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?
GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-GlcNAc beta-(1,3)-Galbeta-(1,4)-Glcbeta-O-C3H6-biotin
?
show the reaction diagram
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i.e. 3'SLNL
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?
GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-GlcNAc beta-O-BSA-biotin
?
show the reaction diagram
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i.e. 3'SLN-BSA
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?
GDP-beta-L-fucose + Neu5Ac alpha(2,3)-Galbeta(1,4)-GlcNAc beta-O-C3H6-biotin
?
show the reaction diagram
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i.e. 3'SLN
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?
GDP-beta-L-fucose + Neu5Acalpha-(2,3)-Galbeta-(1,4)-GlcNAcbeta-R
GDP + Neu5Acalpha-(2,3)-Galbeta-(1,4)-[Fucalpha-(1,3)]-GlcNAcbeta-R
show the reaction diagram
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the last step in sLex epitope formation is catalyzed byalpha(1,3)-fucosyltransferase VII, i.e. FucTVII, which transfers a fucosyl moiety from GDP-fucose to the core oligosaccharide structures, overview
i.e. antigen sLex
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?
GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3]-GlcNAc-R
show the reaction diagram
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sialyl-Lewisx terminal structure
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?
GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)[SO3H-6]-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3][SO3H-6]-GlcNAc-R
show the reaction diagram
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sialyl-Lewisx terminal structure
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?
GDP-beta-L-fucose + NeuAcalpha2,3Galbeta1,4GlcNAc
?
show the reaction diagram
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32% of the activity with Galbeta1,4GlcNAc
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?
GDP-beta-L-fucose + NeuNAcalpha(2->3)Galbeta(1->4)GlcNAc
GDP + NeuNAcalpha(2->3)Galbeta(1->4)[L-Fucalpha(1->3)]GlcNAc
show the reaction diagram
best substrate
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?
GDP-beta-L-fucose + octyl Galbeta(1->4)GlcNAc
GDP + octyl Galbeta(1->4)[L-Fucalpha(1->3)]GlcNAc
show the reaction diagram
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?
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
show the reaction diagram
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?
GDP-fucose + (-3GalNAcbeta1-4GlcNAcbeta1-)n
GDP + (-3GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-)n
show the reaction diagram
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N-glycans containing poly-LDN structures are efficiently fucosylated by human FucT9 producing poly-LDNF structures, max. 4-6 repeating LDNF units
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?
GDP-fucose + (Galbeta1-4Galbeta1-4GlcNAcbeta1-2Manalpha1-6[Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3])Manbeta1-4GlcNAc
GDP + (Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-6[Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3])Manbeta1-4GlcNAc
show the reaction diagram
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oligosaccharides are determined by a combination of exoglycosidase digestions and two-dimensional HPLC sugar mapping, most of these oligosaccharides are free form
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?
GDP-fucose + (Galbeta1-4Galbeta1-4GlcNAcbeta1-2Manalpha1-6[Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3])Manbeta1-4GlcNAcbeta1-4GlcNAc
GDP + (Galbeta1-4Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-6[GalbetaGalbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3])Manbeta1-4GlcNAcbeta1-4GlcNAc
show the reaction diagram
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?
GDP-fucose + asialo human erythropoietin
GDP + fucosylated asialo human erythropoietin
show the reaction diagram
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?
GDP-fucose + bovine asialofetuin
GDP + fucosylated bovine asialofetuin
show the reaction diagram
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?
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAc
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc
show the reaction diagram
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc-O-(CH2)3NHCO(CH2)5-biotin
show the reaction diagram
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-
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?
GDP-fucose + Fucalpha1-2Galbeta1-4GlcNAcbeta1-R
GDP + Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-R
show the reaction diagram
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Lewis Y antigen, increased expression in cancer cells
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?
GDP-fucose + Galbeta(1,3)GlcNAcOMe
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcOMe
show the reaction diagram
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-
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?
GDP-fucose + Galbeta1-4Glc
GDP + Galbeta1-4 (Fucalpha1-3)Glc
show the reaction diagram
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?
GDP-fucose + Galbeta1-4Glc-NAc-O-(CH2)3NHCO(CH2)5-NH-biotin
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
show the reaction diagram
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-
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GDP-fucose + Galbeta1-4GlcNAc
GDP + Galbeta1-4 (Fucalpha1-3)GlcNAc
show the reaction diagram
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-
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?
GDP-fucose + Galbeta1-4GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-O-(CH2)3NHCO(CH2)5-NH-biotin
show the reaction diagram
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sFUT9 efficiently fucosylates type II acceptors but not the corresponding sialylated acceptors, and only very poorly the type I (Galbeta3GlcNAc-R) related acceptors
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?
GDP-fucose + Galbeta1-4GlcNAc-R
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc-R
show the reaction diagram
GDP-fucose + Galbeta1-4GlcNAcbeta1-2Manalpha1-6(Galbeta1-4GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-Asn
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-6(Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-Asn
show the reaction diagram
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-
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?
GDP-fucose + Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-PA
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc-PA
show the reaction diagram
Lacto-N-neo-tetraose is a Lewis-type FucT substrate
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-
?
GDP-fucose + GalNAcbeta1-4GlcNAcbeta-R
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-R
show the reaction diagram
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-
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?
GDP-fucose + GalNAcbeta1-4GlcNAcbeta1-2Manalpha1-6(GalNAcbeta1-4GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-Asn
GDP + GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-6(GalNAcbeta1-4(Fucalpha1-3)GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-Asn
show the reaction diagram
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-
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?
GDP-fucose + GalNAcbeta1-4GlcNAcbeta1-3Galbeta1-4Glc
GDP + GalNAcbeta1-4[Fucalpha1-3]GlcNAcbeta1-3Galbeta1-4Glc
show the reaction diagram
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incubation with extracts from transfected COS7 cells
product obtained at a level of about 50% of that obtained with the acceptor GalNAcbeta1-4GlcNAcbeta1-R
?
GDP-fucose + GalNAcbeta1-4GlcNAcbeta1-R
GDP + GalNAcbeta1-4[Fucalpha1-3]GlcNAcbeta1-R
show the reaction diagram
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-
-
?
GDP-fucose + human erythropoietin
GDP + fucosylated human erythropoietin
show the reaction diagram
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-
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?
GDP-fucose + LacNAc
GDP + ?
show the reaction diagram
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-
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?
GDP-fucose + LacNAcbeta-O-(CH2)5CO2CH3
GDP + ?
show the reaction diagram
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-
-
?
GDP-fucose + lacto-N-neotetraose
GDP + ?
show the reaction diagram
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-
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?
GDP-fucose + lacto-N-neotetraose
GDP + lacto-N-fucopentaose III
show the reaction diagram
GDP-fucose + methyl beta-D-2-O-methylgalactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
GDP + methyl beta-D-2-O-methylgalactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
GDP-fucose + methyl beta-D-2-O-methylgalactosyl-(1-4)-6-O-methyl-N-acetyl-beta-D-glucosamine
GDP + methyl beta-D-2-O-methylgalactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-6-O-methyl-N-acetyl-beta-D-glucosamine
show the reaction diagram
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-
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?
GDP-fucose + methyl beta-D-2-O-methylgalactosyl-(1-4)-N-acetyl-beta-D-glucosamine
GDP + methyl beta-D-2-O-methylgalactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-N-acetyl-beta-D-glucosamine
show the reaction diagram
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-
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?
GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-acetylamino-beta-D-glucopyranose
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-acetylamino-beta-D-glucopyranose
show the reaction diagram
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-
-
-
?
GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-amino-beta-D-glucopyranose
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-amino-beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
show the reaction diagram
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-
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?
GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-methylsulfonylamino-beta-D-glucopyranose
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-6-deoxy-6-methylsulfonylamino-beta-D-glucopyranose
show the reaction diagram
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-
-
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?
GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl amide
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl amide
show the reaction diagram
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-
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?
GDP-fucose + methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl ester
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl ester
show the reaction diagram
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-
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-
?
GDP-fucose + methyl beta-D-galactosyl-(1-4)-6-O-methyl-N-acetyl-beta-D-glucosamine
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-6-O-methyl-N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
GDP-fucose + methyl beta-D-galactosyl-(1-4)-6-O-methylsulfonyl-N-acetyl-beta-D-glucosamine
GDP + methyl beta-D-galactosyl-(1-4)-[alpha-D-fucosyl-(1-3)]-6-O-methylsulfonyl-N-acetyl-beta-D-glucosamine
show the reaction diagram
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-
-
-
?
GDP-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc
GDP + NeuAcalpha2-3Galbeta1-4(Fucalpha1-3)GlcNAc
show the reaction diagram
GDP-fucose + sialyl-alpha-2,3-N-acetyllactosamine
GDP + NeuNAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAc
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + 2'-fucosyllactose
GDP + ?
show the reaction diagram
42% of the activity with Galbeta(1,4)GlcNAc
-
-
?
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
show the reaction diagram
-
-
-
?
GDP-L-fucose + 3'-sialyl N-acetyl lactosamine
GDP + ?
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + alpha(2,3)-sialyllactosamine
GDP + ?
show the reaction diagram
-
115% of the activity with Galbeta(1,4)GlcNAc
-
-
?
GDP-L-fucose + alpha(2,3)sialyllactosamine
GDP + ?
show the reaction diagram
-
-
-
?
GDP-L-fucose + alpha1 acid glycoprotein
GDP + ?
show the reaction diagram
-
with the major terminal structure on N-linked chains: NeuAc(2,3/6)Galbeta(1,4)GlcNAcbeta-R
-
-
?
GDP-L-fucose + asialo-alpha1-acid glycoprotein
GDP + ?
show the reaction diagram
-
with the major terminal structure on N-linked chains: Galbeta(1,4)GlcNAcbeta-R
-
-
?
GDP-L-fucose + asialo-fetuin
GDP + ?
show the reaction diagram
-
with the major terminal structure on N-linked chains: Galbeta(1,4)GlcNAcbeta-R
-
-
?
GDP-L-fucose + asialotransferrin
GDP + ?
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + desialylated alpha1-acid glycoprotein
GDP + ?
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + fetuin
GDP + ?
show the reaction diagram
GDP-L-fucose + fetuin
GDP + alpha1,3-L-fucosyl-fetuin
show the reaction diagram
-
FucT-VI
-
-
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,3)GlcNAc-R
GDP + ?
show the reaction diagram
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)Glc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))Glc
show the reaction diagram
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAc
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
show the reaction diagram
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAcbeta(CH2)8COOMe
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(CH2)8COOMe
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + Fucalpha(1,2)Galbeta(1,4)GlcNAcbeta-bovine-serum-albumin
GDP + Fucalpha(1,2)Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta-bovine-serum-albumin
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + Galalpha(1,3)Galbeta(1,4)GlcNAc-R
GDP + ?
show the reaction diagram
GDP-L-fucose + Galbeta(1,3)GlcNAc
GDP + ?
show the reaction diagram
i.e. lacto-N-biose I, 10% of the activity with Galbeta(1,4)GlcNAc
-
-
?
GDP-L-fucose + Galbeta(1,4)-Glc
GDP + Galbeta(1,4)(Fucalpha(1,3))Glc
show the reaction diagram
-
3% of the activity with Galbeta(1,4)GlcNAc
-
-
?
GDP-L-fucose + Galbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc
show the reaction diagram
GDP-L-fucose + Galbeta(1,4)GlcNAc-O(CH2)8CO2CH3
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-O(CH2)8CO2CH3
show the reaction diagram
GDP-L-fucose + Galbeta(1,4)GlcNAc-R
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAc-R
show the reaction diagram
GDP-L-fucose + Galbeta(1,4)GlcNAcbeta(1,2)Manalpha(1,6)Manbeta(1,4)GlcNAc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,2)Manalpha(1,6)Manbeta(1,4)GlcNAc
show the reaction diagram
-
-
-
-
-
GDP-L-fucose + Galbeta(1,4)GlcNAcbeta(1,3)Galbeta(1,4)Glc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,3)Galbeta(1,4)Glc
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + Galbeta(1,4)GlcNAcbeta(1,3)Galbeta(1,4)Glc
GDP + Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,3)Galbeta(1,4)Glc + Galbeta(1,4)GlcNAcbeta(1,3)Galbeta(1,4)(Fucalpha(1,3))Glc
show the reaction diagram
-
-
-
-
GDP-L-fucose + lacto-N-biose I
GDP + ?
show the reaction diagram
-
-
-
?
GDP-L-fucose + lacto-N-fucopentaose I
GDP + ?
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + lacto-N-fucopentaose II
GDP + ?
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + lacto-N-neotetraose
GDP + Galbeta1-4(Fucalpha1-3)GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine
show the reaction diagram
-
-
-
?
GDP-L-fucose + lacto-N-tetraose
GDP + ?
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + lactose
GDP + ?
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
GDP-L-fucose + NeuAcalpha(2,3)Galbeta(1,4)GlcNAc
GDP + NeuAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAc
show the reaction diagram
GDP-L-fucose + NeuAcalpha(2,3)Galbeta(1,4)GlcNAcbeta(1,2)Manalpha(1,6)Manbeta(1,4)GlcNAc
GDP + NeuAcalpha(2,3)Galbeta(1,4)(Fucalpha(1,3))GlcNAcbeta(1,2)Manalpha(1,6)Manbeta(1,4)GlcNAc
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + sialyl-alpha-2,3-LacNAc-O-(CH2)3-N-dansyl
GDP + Galbeta(1-4)-[Fucalpha(1-3)]GlcNAc-O-(CH2)3-N-dansyl
show the reaction diagram
-
-
-
-
?
GDP-L-fucose + sialyl-alpha-2,3-N-acetyllactosamine
GDP + NeuNAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAc
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-beta-fucose + alpha2,3-sialyl N-acetyllactosaminyl-R
GDP + alpha1,3-fucosyl-alpha2,3-sialyl-N-acetyllactosaminyl-R
show the reaction diagram
-
FucT-VII and FucT-IV
-
-
?
GDP-beta-L-fucose + asialo-erythropoietin
?
show the reaction diagram
-
wild-type FUT9 efficiently fucosylates di-, tri- and tetraantennary N-glycans from asialoEPO
-
-
?
GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R
GDP + beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-R
show the reaction diagram
-
-
-
-
?
GDP-beta-L-fucose + N-acetyllactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
show the reaction diagram
GDP-beta-L-fucose + Neu5Acalpha-(2,3)-Galbeta-(1,4)-GlcNAcbeta-R
GDP + Neu5Acalpha-(2,3)-Galbeta-(1,4)-[Fucalpha-(1,3)]-GlcNAcbeta-R
show the reaction diagram
-
the last step in sLex epitope formation is catalyzed byalpha(1,3)-fucosyltransferase VII, i.e. FucTVII, which transfers a fucosyl moiety from GDP-fucose to the core oligosaccharide structures, overview
i.e. antigen sLex
-
?
GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3]-GlcNAc-R
show the reaction diagram
-
sialyl-Lewisx terminal structure
-
-
?
GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)[SO3H-6]-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3][SO3H-6]-GlcNAc-R
show the reaction diagram
-
sialyl-Lewisx terminal structure
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
alternative divalent metal cofactor
MnCl2
-
glycosyltransferase assay with 20 mM MnCl2
additional information
-
CEFT-3 does not require divalent cations, while CEFT-4 is activates by some divalent cations, with slight prefernce for Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethynylnaphthalene
-
exhibits highly potent inhibitory effects against the FUT-VI mediated sialyl Lewis X synthesis
6-F-GDP-fucose
-
complete inhibition
deoxyfuconojirimycin
-
modest inhibitor, causes 21% inhibition, synergism: combined with GDP at their Ki levels results in 80% inhibition, combined with GMP causes 50.4% inhibition
diethyldicarbonate
dithionitrobenzene
-
-
GDP-(1-[2-[(naphthalen-1-ylmethyl)-carbamoyl]-ethyl]-1H-[1,2,3]triazol-4-ylmethyl)
-
-
GDP-alpha-D-glucose
-
-
GDP-alpha-D-mannose
-
-
GDP-choline
-
0.5 mM, 90% inhibition
GDP-fucose
GDP-hexanolamine
-
-
GDP-[1-[(1,2-diphenyl-ethylcarbamoyl)-methyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
GDP-[1-[3-(1,2-diphenyl-ethylcarbamoyl)-butyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
GDP-[1-[3-(1,2-diphenyl-ethylcarbamoyl)-propyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
GDP-[1-[4-(9,10-dioxo-9,10-dihydro-anthracen-2-ylcarbamoyl)-butyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
GTP
-
potent inhibitor
Inosine diphosphate
-
potent inhibitor
L-fucal
-
modest inhibitor, causes 26% inhibition, combined with GDP causes 40% inhibition
-
N-bromosuccinimide
-
moderate inhibition
N-ethylmaleimide
NaCl
-
40% inhibition at 300 mM
Neu5(OHAc)alpha(2-3)Galbeta(1-4)GlcNAc-beta-(3-amino)propyl
-
-
Neu5Acalpha(2-3)Galbeta(1-4)6-deoxyGlcNAc-beta-methyl
-
-
Neu5Acalpha(2-3)Galbeta(1-4)6-sulfoGlcNAc-beta-methyl
-
-
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta(1-3)LacN-(2-acetamido)ethyl
-
-
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta(1-6)GalNAc-(2-acetamido)ethyl
-
-
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta-(3-amino)propyl
-
-
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta-biphenyl-4-carboxylic acid propyl amide
-
-
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta-methyl
-
-
Ni2+
-
inhibits CEFT-4
tunicamycin
inhibits N-glycosylation of the enzyme in recombinant COS-7 cells which leads to inactivation of rFuc-TVII
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-mercaptoethanol
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65
3'-sialyl N-acetyl lactosamine
-
pH 7.2, 37°C
0.00094
6-deoxy-6-N-(2-naphthalene-2-yl-acetamide)-beta-L-galactopyranos-1-yl-guanosine 5'-diphosphate disodium salt
-
pH 7.5, 25°C
1.4
6-deoxy-alpha-L-galactopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranose
-
pH 7.6, 15 mM MnCl2, 0.095 mM GDP-fucose
-
0.38
alpha(2,3) bisialylated biantennary glycan
-
pH 7.2, 37°C
-
7.8
alpha2,3-sialyl-N-acetyllactosamine
-
pH 6.5, 30°C, recombinant FucT-VII
6.7
Ca2+
-
-
1.2
Co2+
-
-
72 - 543
D-lactose
6.7 - 20
Fucalpha(1,2)Galbeta(1,4)Glc
0.7 - 3.9
Fucalpha(1,2)Galbeta(1,4)GlcNAc
1
Fucalpha1-2Galbeta1-4Glc
-
-
17
Gal-beta-(1->3)-[Fuc-alpha-(1->4)-])GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
pH 7.6, 15 mM MnCl2, 0.095 mM GDP-fucose
0.35
Galbeta(1,3)GlcNAcOMe
-
-
25
Galbeta(1,4)Glc
-
-
1.4 - 23
Galbeta(1,4)GlcNAc
1.5
Galbeta(1,4)GlcNAcbeta(1,3)Galbeta(1,4)Glc
-
pH 7.3, 37°C
0.37 - 1.7
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
8.1
Galbeta1-4Glc
-
-
0.4
Galbeta1-4GlcNAc
-
-
0.021
GDP-beta-fucose
-
pH 6.5, 30°C, recombinant FucT-VII and commercial FucT-VI
0.00012 - 1.12
GDP-beta-L-fucose
0.0016 - 0.06
GDP-fucose
0.0055 - 0.062
GDP-L-fucose
8.8
LacNAc
-
-
0.17
LacNAcbeta-O-(CH2)5CO2CH3
-
-
0.3 - 0.76
lacto-N-neotetraose
5
lacto-N-tetraose
-
pH 7.6, 15 mM MnCl2, 0.095 mM GDP-fucose
83
lactose
-
pH 7.6, 15 mM MnCl2, 0.095 mM GDP-fucose
0.075
methyl beta-D-2-O-methylgalactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
-
-
0.12
methyl beta-D-2-O-methylgalactosyl-(1-4)-6-O-methyl-N-acetyl-beta-D-glucosamine
-
-
0.39
methyl beta-D-2-O-methylgalactosyl-(1-4)-N-acetyl-beta-D-glucosamine
-
-
0.19
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-acetylamino-beta-D-glucopyranose
-
-
0.4
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-amino-beta-D-glucopyranose
-
-
0.14
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-formylamino-beta-D-glucopyranose
-
-
0.115
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-6-deoxy-6-methylsulfonylamino-beta-D-glucopyranose
-
-
1.54
methyl beta-D-galactosyl-(1-4)-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl amide
-
-
0.29
methyl beta-D-galactosyl-(1-4)-6-O-methyl-N-acetyl-beta-D-glucosamine
-
-
0.25
methyl beta-D-galactosyl-(1-4)-6-O-methylsulfonyl-N-acetyl-beta-D-glucosamine
-
-
0.45
methyl beta-D-galactosyl-(1->4)-2-deoxy-2-acetylamino-beta-D-glucopyranosiduronic acid methyl ester
-
-
8.6
Mg2+
-
-
6.1
Mn2+
-
-
2.6
N-acetyl lactosamine
-
pH 7.2, 37°C
0.53
N-acetyl-beta-lactosamine
-
-
0.0026 - 0.61
N-acetyllactosamine
0.05
Neu5Acalpha(2,3)-Galbeta(1,4)-6-O-sulfo-GlcNAc beta-O-C3H6-biotin
-
pH 7.4, 22°C
3.9
NeuAcalpha(2,3)Galbeta(1,4)Glc
-
-
0.2 - 0.9
NeuAcalpha(2,3)Galbeta(1,4)GlcNAc
0.96
NeuAcalpha2-3Galbeta1-4GlcNAc
-
-
1.7
sialyl-alpha-2,3-N-acetyllactosamine
-
fusion protein Hsp150delta-FucTe
0.74
unsialylated biantennary glycan
-
pH 7.2, 37°C
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.25 - 5.97
D-lactose
1.7 - 3.6
Fucalpha(1,2)Galbeta(1,4)GlcNAc
1.1 - 2.3
Galbeta1,4GlcNAc-O(CH2)8CO2CH3
0.063 - 2.3
GDP-beta-L-fucose
0.042 - 0.12
N-acetyllactosamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 0.083
D-lactose
3242
0.191 - 5.041
GDP-beta-L-fucose
651
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002
6-F-GDP-fucose
-
pH 7.4, 22°C
45
deoxyfuconojirimycin
-
-
0.0045 - 0.029
GDP
0.000901
GDP-(1-[2-[(naphthalen-1-ylmethyl)-carbamoyl]-ethyl]-1H-[1,2,3]triazol-4-ylmethyl)
-
-
0.38
GDP-alpha-D-glucose
-
-
0.29
GDP-alpha-D-mannose
-
-
0.0062 - 0.031
GDP-fucose
0.000437
GDP-[1-[(1,2-diphenyl-ethylcarbamoyl)-methyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
0.000376
GDP-[1-[3-(1,2-diphenyl-ethylcarbamoyl)-butyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
0.001069
GDP-[1-[3-(1,2-diphenyl-ethylcarbamoyl)-propyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
0.000511
GDP-[1-[4-(9,10-dioxo-9,10-dihydro-anthracen-2-ylcarbamoyl)-butyl]-1H-[1,2,3]triazol-4-ylmethyl]
-
-
0.7
GMP
-
-
0.069
Inosine diphosphate
-
-
71
L-fucal
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0054
1-ethynylnaphthalene
Homo sapiens
-
-
0.00064
6-F-GDP-fucose
Homo sapiens
-
pH 7.4, 22°C
0.092
diethyldicarbonate
Homo sapiens
-
IC50: 0.092 mM. Preincubation at 23°C gives maximal inhibition, 75%, after 180 s. Preincubation at 13°C gives 55% inhibition after 3 min. Preincubation at 4°C results in only 35% inhibition
0.035
Neu5(OHAc)alpha(2-3)Galbeta(1-4)GlcNAc-beta-(3-amino)propyl
Homo sapiens
-
pH 7.4, 22°C
0.0279
Neu5Acalpha(2-3)Galbeta(1-4)6-deoxyGlcNAc-beta-methyl
Homo sapiens
-
pH 7.4, 22°C
0.0104
Neu5Acalpha(2-3)Galbeta(1-4)6-sulfoGlcNAc-beta-methyl
Homo sapiens
-
pH 7.4, 22°C
0.0838
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta(1-3)LacN-(2-acetamido)ethyl
Homo sapiens
-
pH 7.4, 22°C
0.0347
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta(1-6)GalNAc-(2-acetamido)ethyl
Homo sapiens
-
pH 7.4, 22°C
0.227
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta-(3-amino)propyl
Homo sapiens
-
pH 7.4, 22°C
0.0143
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta-biphenyl-4-carboxylic acid propyl amide
Homo sapiens
-
pH 7.4, 22°C
0.0516
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-beta-methyl
Homo sapiens
-
pH 7.4, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000002
-
-
0.000017
substrate sialyl-N-acetyllactosamine
0.002289
-
-
0.067
-
mutant enzyme N101Q, at pH 4.5 and 37°C
0.154
-
mutant enzyme N62Q, at pH 4.5 and 37°C
0.248
-
wild type enzyme, at pH 4.5 and 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.5
-
recombinant FucT-VII
6
-
soluble enzyme
6.2
-
membrane-bound enzyme
6.25
-
-
7 - 8
-
reaction with N-acetyllactosamine
7.2 - 8
-
-
7.4
-
assay at
7.6 - 8
-
-
8.5
maximal activity at pH 6.5 or 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.8
-
pH 6.0: about 40% of maximal activity, pH 8.8: about 50% of maximal activity, reaction with N-acetyllactosamine
6.5 - 9
pH range for FucTC is very broad
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
-
glycosyltransferase assay
25
-
assay at
30
-
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 50
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
transcript of FUT6 mRNA detected
Manually annotated by BRENDA team
-
from patients suffering from cystic fibrosis
Manually annotated by BRENDA team
-
at the segmentation period, at 12, 18 and 48 h after fertilization
Manually annotated by BRENDA team
-
FUT7 mRNA minorly expressed in mouse brain endothelial cell line bEND.3
Manually annotated by BRENDA team
-
the enzyme is expressed in endothelial cells lining the high endothelial venules of perpheral lymph nodes, mesenteric lymph nodes and Pever‘s patches
Manually annotated by BRENDA team
-
FT-IV mRNA is the predominant transcript in eosinophils isolated from human blood, TGF-beta1 upregulates FT-IV mRNA expression; FT-VII mRNA is weakly expressed in eosinophils isolated from human blood, its expression is up-regulated by TGF-beta1 to some extent
Manually annotated by BRENDA team
-
eosinophilic; neutrophilic
Manually annotated by BRENDA team
-
FUT4 mRNA is prominently expressed in Jurkat cells, a human T cell line, FUT4 and FUT9 mRNA are distinctly up-regulated in Jurkat cells 3 h and 12 h after granzyme B treatment, respectively, whereas other FUT mRNAs are not affected; FUT9 mRNA is scarcely expressed in Jurkat cells, a human T cell line, FUT4 and FUT9 mRNA are distinctly up-regulated in Jurkat cells 3h and 12 h after granzyme B treatment, respectively, whereas other FUT mRNAs are not affected
Manually annotated by BRENDA team
rFuc-TVII mRNA expression strongly detected in rat lymph node
Manually annotated by BRENDA team
-
FUT7 mRNA remarkably highly expressed in mouse lymphoid tumor cell line TIB-63
Manually annotated by BRENDA team
-
FUT7 mRNA significantly expressed in mouse macrophage cell line TIB-69
Manually annotated by BRENDA team
NTERA-2/cl.D1 cells are cultured and differentiated into NT2N neurons
Manually annotated by BRENDA team
predominantly expressed
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
hsp150delta-FucTe fusion protein remains mostly non-covalently attached to the cell wall
Manually annotated by BRENDA team
-
granules of endothelial cells (Weibel-Parade bodies)
Manually annotated by BRENDA team
-
TI-VAMP, compartment of NT2N neurons
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37800
-
after PNGaseF treatment
38000
-
x * 38000, SDS-PAGE
39200
-
x * 39200, estimated from SDS-PAGE
40680
-
x * 40680, SDS-PAGE
41300
-
SDS-PAGE, sFUT9
41892
1 * 41892, calculation from nucleotide sequence
43008
-
1 * 43008, calculation from nucleotide sequence
43034
1 * 43034, calculation from nucleotide sequence
45000
-
gel filtration
50556
1 * 50556, calculation from nucleotide sequence
51200
-
x * 51200, alpha-(1,3/1,4)-fucosyltransferase(1-428), calculated from sequence; x * 51200, mutant alpha-(1,3/1,4)-fucosyltransferase (1–441), calculated from sequence
54000
-
x * 54000, glycosylated FUT9, SDS-PAGE, x * 47000, deglycosylated FUT9, SDS-PAGE
56700
-
x * 56700, FLAG-tagged enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
-
the enzyme possesses a cytoplasmic domain, a transmembrane domain, and a large Golgi lumenal catalytic domain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
FucTVII is very stable against freeze/thaw cycles
-
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(1–441) loses 38% activity after 3 months
-
most stable at -80°C with or without glycerol supplementation
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; alpha-(1,3/1,4)-fucosyltransferase(1–428) with a His6 tag at the C terminus is purified
-
affinity column chromatography
-
native enzyme by preparation of microsome and Golgi membrane fractions, ultracentrifugation, and affinity chrotography
-
Ni-NTA column chromatography
-
partial
-
recombinant FucT-VII catalytic domain-protein A fusion protein from Sf21 insect cells by IgG affinity chromatography
-
soluble enzyme
-
using ammonium sulfate precipitation, hydrophobic chromatography in phenyl-Sepharose, ion-exchange chromatography on sulfopropyl-Sepharose, affinity chromatography on GDP-heanolamine-Sepharose, and finally high pressure liquid chromatography gel filtration
-
using method A: column chromatography on DEAE-Sephadex, SP-Sephadex, ASTD-Sepharose and GTP-Agarose, method B: column chromatography on DEAE-Sephacel, SP-Sephadex and Synsorb-Galbeta1-4GlcNAc
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; full-length and each truncated FucT (DELTAFucT) are expressed in Escherichia coli HMS174DE3
-
applying a baculovirus system in Spodoptera frugiperda Sf9 cells; expressed in Sf9 insect cells
-
CEFT DNA and amino acid sequence determination and analysis, expression analysis, expression in COS-7 cells
-
cloning of rat Fuc-TVII gene which is expressed as two splice variants, but only the long one shows enzymatic activity, expression of the long splice variant in COS-7 cells
COS-7 cells transiently transfected with Fuc-TVII expression vectors
-
expressed in complex with green fluorescent protein in HEK cells
-
expressed in COS-1 cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BW25113 (DE3) cells
-
expression in CHO cells, to confirm the hypothesis that FucT-VII and keratin sulfate sulfotransferase (KSST) may compete for the same acceptor molecules FucT-VII and Core2GlcNAcT-1 are expressed in CHO cells stably expressing KSST, sialyl Lewis X expression is significantly reduced in these cells
-
expression in CHO cells; poly-LDN backbone is efficiently fucosylated by recombinant human alpha1,3-fucosyltransferase IX (FucT 9) when it is stably co-expressed with the Cebeta4GalNAcT in cell line L8-GalNAcT-FucT
-
expression in COS cells
-
expression in hepatocellular carcinoma H7721 cells, alpha1,3FucT-VII acts as a potential antiapoptotic factor in H7721 cells after induction of apoptosis by UV irradiation, increasing phosphorylated JNK, quantitative real-time PCR analysis of expression of enzyme product SLex, overview
-
expression in Pichia pastoris
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 in Pichia pastoris; expression in Saccharomyces cerevisiae
-
expression of FucTVII catalytic domain in HEK-293 cells
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FucT-VII-/-GFP+ bone marrow transplanted into lethally irradiated low-density lipoprotein receptor low density lipoprotein receptor mice or FucT-VII+/+GFP+ bone marrow into FucT-VII-/-, low density lipoprotein receptor double-mutant mice
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FucT-VII: DNA and amino acid sequence determination and analysis, expression of the catalytic domain of FucT-VII fused to protein A from Staphylococcus aureus in Spodoptera frugiperda Sf21 insect cells via the baculovirus infection system
-
full-length form of human FUT9 and a truncated form containing sFUT9 the catalytic domain of the enzyme are overexpressed in Spodoptera frugiperda (Sf9) insect cells using the signal sequence of human interleukin 2 for efficient secretion, high activity of the trunctated, soluble form sFUT9 in the supernatant of Sf9 cells, sFUT9 fucosylates sialylated and non-sialylated glycoproteins
-
fusion construct consisting of maltose-binding protein and soluble FucT-IX overexpressed in Escherichia coli. Constitutive expression of FucT-IX in Sf9 insect cells, different recombinant baculoviruses containing the N-terminal signal sequences from gp67and beta-trace proteins followed by a histidine tag fused to the soluble FucT-IX-encoding sequence, respectively, and infection of Sf9 cells
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FUT9, DNA and amino acid sequence determination and analysis, transient overexpression of His-tagged or V5-tagged wild-type and mutant FUT9 proteins in HeLa cells
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gene fragment encoding the catalytic domain comprising residues 38–359 of FUT9a fused N-terminally with the sequence encoding the first 53 aa of the Arabidopsis thaliana XylT gene. Hybrid gene placed under control of the Cassava Vein Mosaic virus promoter, and the resulting expression cassette combined with the one comprising the hybrid GalT under control of the CaMV 35S promoter. Transferred to a plant transformation vector conferring hygromycin resistance, which is designated xFxG
gene FUT11, expression analysis in bronchial mucosa of cystic fibrosis patients
-
into the vector pET-24b+ for expression in Escherichia coli cells
overexpression in A-431 cells cells, two stable FUT-4 cell lines A431-FUT4-1 and A431-FUT4-2
-
putative cDNA amplified by PCR from a cDNAlambdaZAP library, cloned into the mammalian expression vector pCR3.1 and sequenced, transfection of COS7 kidney cells from the African green monkey with cDNA encoding the enzyme results in about 20fold level of activity over control cells, using lacto-N-neotetraose as acceptor
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regions 5' of the FUT VI transcription start site, -2,067 to +1 nt and -2,067 to +213 nt isolated, PCR products 5'-phosphorylated using the T4 polynucleotide kinase and then ligated into pGL4.11 vector digested with EcoRV and treated with alkaline phosphatase from Escherichia coli. Plasmids transiently transfected into HepG2 and HuH-7 cells
-
transfection of COS-1 and CHO-T cells
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truncated constructs lacking the transmembrane region and the cytosolic N-terminus, are expressed in baculovirus-infected Trichoplusia ni insect cells and in two non-lytic expression systems, stably transfect human HEK 293 and Trichoplusia ni cells. Since secretion of some glycosyltransferases is controlled by formation of dimeric molecules via disulfide bonds, one of the fucosyltransferase V constructs contains the N-terminal cysteine residue 64 for dimerization, whereas this residue is replaced in the other construct by serine
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
breast cancer cell lines display increased expression of isoform FUT4
-
FUT4 mRNA is significantly upregulated during the early and midsecretory stages of the menstrual cycle compared with the other menstrual phases, with maximal expression during the mid-secretory phase. In proliferative explants, progesterone significantly increases FUT4 transcription and translation after 24 h in culture. Estrogen does not have any significant effects
-
FUT4 staining is weak in proliferative and menstrual endometrium. Inductive effect of progesterone on FUT4 transcription is lost after 48 h of treatment
-
higher mRNA and protein expression of the enzyme are observed in colorectal tumors compared with adjacent normal ones
-
in hepatocellular carcinoma tissues, the expression levels and activity of alpha1,3/4-fucosyltransferase FUT6 are significantly up-regulated
-
protein kinase R function is essential for FUT3, FUT5, and FUT6 induction and sLex expression in Herpes simplex virus type 1-infected cells. IMD-0354, an inhibitor of the NF-kappaB-activating factor IKK-2, induces FUT transcription via a IKK-2-independent mechanism, irrespective of whether the cells are virus-infected or not
-
protein kinase R inhibitors 2-aminopurine and C16 inhibit FUT3, FUT5, and FUT6 expression. MG-132 inhibits the IMD-0354-dependent transcription of FUT5 in a dose-dependent manner
-
two hepatocyte nuclear factor-4alpha (HNF-4alpha) and one octamer binding transcription factor-1 (Oct-1) binding sites are essential for FUT VI transcription, which are the 5'-flanking regions at positions -156 to -136 nt and -56 to -19 nt relative to the FUT VI gene transcription start site. Transient overexpression of HNF-4alpha but not Oct-1 enhances both FUT VI promoter activities and FUT VI mRNA levels in HuH-7 cells. FUT VI mRNA levels are higher in HepG2 cells than in HNF-4alpha-transfected HuH-7 cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R115W/E116D
-
double mutation slightly increases H-type 1 activity
A128N
-
the mutant displays 3.4fold higher catalytic activity with D-lactose than the wild type enzyme
A128N/H129E
-
the mutant displays 6.5fold higher catalytic activity with D-lactose than the wild type enzyme
A128N
-
the mutant displays 3.4fold higher catalytic activity with D-lactose than the wild type enzyme
-
A128N/H129E
-
the mutant displays 6.5fold higher catalytic activity with D-lactose than the wild type enzyme
-
A349D
-
mutant enzyme shows higher activity with a range of acceptor substrates, higher affinity for Fucalpha(1,2)Galbeta(1,4)GlcNAc, 8fold higher overall catalytic efficiency than that of wild-type enzyme. The single amino acid site Asp336 of FucT III and Ala349 of FucT V constitutes the only difference in the sequence of FucT III and V over the final 210 COOH-terminal amino acid residues, impacts the acceptor substrate profiles of FucT III and FuvT V
C104S
-
mutant enzyme is inactive, mutant enzyme produces a series of lower molecular weight bands when characterized by Wester blot and does not bind GDP
C351S
-
mutant enzyme is inactive
C354S
-
mutant enzyme is inactive
C64S
-
FucT V mutant is secreted exclusively as monomer
C94S
-
mutant enzyme is inactive
N101Q
-
the mutant shows about 30% of wild type activity; the mutant still shows about 27% of wild type activity
N101Q/N153Q
-
the mutations lead to an almost complete loss of enzymatic activity
N153Q
-
the mutant almost completely loses enzymatic activity; the mutation leads to an almost complete loss of enzymatic activity
N191Q/N153Q
-
the mutant almost completely loses enzymatic activity
N62Q
-
the mutant shows about 60% of wild type activity; the mutant still shows about 62% of wild type activity
N62Q/N101Q
-
the mutant almost completely loses enzymatic activity; the mutations lead to an almost complete loss of enzymatic activity
N62Q/N153Q
-
the mutant almost completely loses enzymatic activity; the mutations lead to an almost complete loss of enzymatic activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
a baculoviral expression system of FucT-IX appears to be a promising strategy for overproduction as compared to overproduction in Escherichia coli or mammalian cells
drug development
medicine
synthesis