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Information on EC 2.4.1.68 - glycoprotein 6-alpha-L-fucosyltransferase and Organism(s) Homo sapiens
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2.4.1.68 glycoprotein 6-alpha-L-fucosyltransferaseIUBMB Comments
This enzyme catalyses a reaction similar to that of EC 2.4.1.214, glycoprotein 3-alpha-L-fucosyltransferase, but transfers the L-fucosyl group from GDP-beta-L-fucose to form an alpha1,6-linkage rather than an alpha1,3-linkage.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
alpha1,6-fucosyltransferase, fucosyltransferase 8, alpha1-6fuct, alpha-1,6-fucosyltransferase, alpha1,6fuct, 6fuct, alpha(1,6)ft, alpha6fuct, alpha(1,6)fucosyltransferase, alpha1,6-fuct, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha1,6-fucosyltransferase
alpha1-6FucT
fucosyltransferase, guanosine diphosphofucose-glycoprotein
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FUT8
GDP-fucose glycoprotein fucosyltransferase
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GDP-fucose-glycoprotein fucosyltransferase
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GDP-L-fuc:N-acetyl-beta-D-glucosaminide alpha1-6fucosyltransferase
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GDP-L-fucose-glycoprotein fucosyltransferase
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GDPfucose glycoprotein fucosyltransferase
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glycoprotein fucosyltransferase
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guanosine diphosphofucose-glycoprotein fucosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-beta-L-fucose + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc]-L-asparaginyl-[protein] = GDP + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc]-L-asparaginyl-[protein]
GDP-beta-L-fucose + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc]-L-asparaginyl-[protein] = GDP + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc]-L-asparaginyl-[protein]
type II transmembrane protein
GDP-beta-L-fucose + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc]-L-asparaginyl-[protein] = GDP + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc]-L-asparaginyl-[protein]
fucosyltransferase gene superfamily
GDP-beta-L-fucose + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc]-L-asparaginyl-[protein] = GDP + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc]-L-asparaginyl-[protein]
alpha-2- and alpha-6-fucosyltransferases, from eukaryotic and prokaryotic origin, are grouped into a superfamily due to structural features and consensus peptide motifs in the catalytic domain
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
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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-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}asparagine) 6-alpha-L-fucosyltransferase
This enzyme catalyses a reaction similar to that of EC 2.4.1.214, glycoprotein 3-alpha-L-fucosyltransferase, but transfers the L-fucosyl group from GDP-beta-L-fucose to form an alpha1,6-linkage rather than an alpha1,3-linkage.
CAS REGISTRY NUMBER
COMMENTARY
9033-08-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-beta-fucose + Gal-N-acetylglucosaminyl-Man5-GlcNAc2-(N-(9-fluorenyl)methoxycarbonyl)asparagine
GDP + L-fucose alpha-1,6 bound to Gal-N-acetylglucosaminyl-Man5-GlcNAc2-(N-(9-fluorenyl)methoxycarbonyl)asparagine
100% yield
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?
GDP-beta-fucose + Gal-N-acetylglucosaminyl-Man5-GlcNAc2-erythropoietin
GDP + L-fucose alpha-1,6 bound to the erythropoitin-linked N-acetylglucosamine of Gal-N-acetylglucosaminyl-Man5 + GDP
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-
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?
GDP-beta-fucose + Man5-GlcNAc2-(N-(9-fluorenyl)methoxycarbonyl)asparagine
GDP + L-fucose alpha-1,6 bound to Man5-GlcNAc2-(N-(9-fluorenyl)methoxycarbonyl)asparagine
30% yield
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?
GDP-beta-L-fucose + Gal-N-acetylglucosaminyl-Man5-GlcNAc2-HIV-1 V3 glycopeptide
GDP + L-fucose alpha-1,6-bound to Gal-N-acetylglucosaminyl-Man5-GlcNAc2-HIV-1 V3 glycoprotein
100% yield
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?
GDP-beta-L-fucose + Man5-GlcNAc2-erythropoietin
GDP + L-fucose alpha-1,6-bound to Man5-GlcNAc2-erythropoietin
FUT8 is able to core-fucosylate Man5GlcNAc2 glycan in vitro in the context of reythropoietin, lacking an unmodified GlcNAc moiety at the alpha1,3-arm, 90% yield
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?
GDP-beta-L-fucose + Man5-GlcNAc2-HIV-1 V3 glycopeptide
GDP + L-fucose alpha-1,6-bound to Man5-GlcNAc2-HIV-1 V3 glycoprotein
50% yield
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?
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->6)]-N-acetyl-beta-D-glucosaminyl]asparagine
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?
GDP-beta-L-fucose + reducing terminal GlcNAc of the core structure of asparagine-linked oligosaccharide
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rapid equilibrium random mechanism
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?
GDP-L-fucose + asialo-agalactotransferrin glycopeptide
GDP + L-fucose alpha-1,6 bound to the asparagine-linked N-acetylglucosamine of the asialo-agalactotransferrin glycopeptide
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-(1,6)]-N-acetyl-beta-D-glucosaminyl)asparagine
alpha1,6-fucosylation, also referred to as core fucosylation, plays an essential role in various pathophysiological events. FUT8 null mice shows severe growth retardation and emphysema-like lung-destruction as a result of the dysfunction of epidermal growth factor and transforming growth factor-beta receptors
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?
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine
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-bi-(4-(2-pyridylamino)butylamine
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine-bi-(4-(2-pyridylamino)butylamine)
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-bi-(4-(2-pyridylamino)butylamine)
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine-bi-(4-(2-pyridylamino)butylamine)
GDP-L-fucose + asialo-agalactotransferrin glycopeptide
GDP + L-fucose alpha-1,6 bound to the asparagine-linked N-acetylglucosamine of the asialo-agalactotransferrin glycopeptide
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?
GDP-L-fucose + asialo-agalactotransferrin glycopeptide
GDP + L-fucose alpha-1,6 bound to the asparagine-linked N-acetylglucosamine of the asialo-agalactotransferrin glycopeptide
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human transferrin
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?
GDP-L-fucose + asialo-agalactotransferrin glycopeptide
GDP + L-fucose alpha-1,6 bound to the asparagine-linked N-acetylglucosamine of the asialo-agalactotransferrin glycopeptide
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biantennary to tetraantennary substrates, with the triantennary substrate showing the highest activity
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?
GDP-L-fucose + asialo-agalactotransferrin glycopeptide
GDP + L-fucose alpha-1,6 bound to the asparagine-linked N-acetylglucosamine of the asialo-agalactotransferrin glycopeptide
biantennary to tetraantennary substrates, with the triantennary substrate showing the highest activity
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?
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine
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?
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine
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ir
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine
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i.e. GnGn-peptide
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?
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine
i.e. GnGn-peptide
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?
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine
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the enzyme does not utilize the reducing terminal GlcNAc for fucose transfer but shows a preference for the third GlcNAc residue from the nonreducing terminus of the acceptor
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ir
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-bi-(4-(2-pyridylamino)butylamine
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine-bi-(4-(2-pyridylamino)butylamine)
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pH 7.0, 37°C, 6 h, reaction stopped by heating at 100°C for 1 min
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?
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-bi-(4-(2-pyridylamino)butylamine
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine-bi-(4-(2-pyridylamino)butylamine)
pH 7.0, 37°C, 6 h, reaction stopped by heating at 100°C for 1 min
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?
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-bi-(4-(2-pyridylamino)butylamine)
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine-bi-(4-(2-pyridylamino)butylamine)
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i.e. GnGn-bi-Asn-PABA, synthetic substrate, fluorescent assay
i.e. GnGnF-bi-Asn-PABA
?
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-bi-(4-(2-pyridylamino)butylamine)
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine-bi-(4-(2-pyridylamino)butylamine)
i.e. GnGn-bi-Asn-PABA, synthetic substrate, fluorescent assay
i.e. GnGnF-bi-Asn-PABA
?
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-bi-(4-(2-pyridylamino)butylamine)
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine-bi-(4-(2-pyridylamino)butylamine)
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acceptor substrate is derived from bovine gamma-globulin
i.e. GnGnF-bi-Asn-PABA
?
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-bi-(4-(2-pyridylamino)butylamine)
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-(1-6)]-N-acetyl-beta-D-glucosaminyl]asparagine-bi-(4-(2-pyridylamino)butylamine)
acceptor substrate is derived from bovine gamma-globulin
i.e. GnGnF-bi-Asn-PABA
?
additional information
?
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beta-D-mannosyl-(1-6)-[alpha-D-mannosyl-(1-3)-]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-N-acetyl-beta-D-glucosaminoyl-asparagine is no substrate
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?
additional information
?
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one of the enzymes involved in the synthesis of N-linked glycans of the GpIIb/IIIa (CD41a) which is present in megakaryocytes and platelets
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?
additional information
?
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GlcNAc, chitobiose and chitotriose do not serve as active substrates
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-
?
additional information
?
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the enzyme catalyzes the transfer of a fucose residue from GDP-fucose to the innermost GlcNAc of hybrid and complex N-linked oligosaccharides via alpha(1,6)linkage
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-
?
additional information
?
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free N-glycans lacking an unmasked alpha-1,3-arm GlcNAc moiety are not FUT8 substrates. Man5GlcNAc2 glycan can be efficiently core-fucosylated by FUT8 in an appropriate protein/peptide context, such as with the erythropoietin protein, a V3 polypeptide derived from HIV-1 gp120, or a simple 9-fluorenylmethyl chloroformate-protected Asn moiety. When placed in the V3 polypeptide context, a mature bi-antennary complex-type N-glycan also can be core-fucosylated by FUT8, albeit at much lower efficiency than the Man5GlcNAc2 peptide
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-beta-L-fucose + 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->6)]-N-acetyl-beta-D-glucosaminyl]asparagine
-
-
-
?
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-(1,6)]-N-acetyl-beta-D-glucosaminyl)asparagine
alpha1,6-fucosylation, also referred to as core fucosylation, plays an essential role in various pathophysiological events. FUT8 null mice shows severe growth retardation and emphysema-like lung-destruction as a result of the dysfunction of epidermal growth factor and transforming growth factor-beta receptors
-
-
?
additional information
?
-
-
one of the enzymes involved in the synthesis of N-linked glycans of the GpIIb/IIIa (CD41a) which is present in megakaryocytes and platelets
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mersalyl
-
5 mM, complete inhibition, inhibition can be very significantly prevented by GDP-fucose, GDP or GnGnGp
methyl (1Z)-N-[[5-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)pentyl]sulfanyl]-3-[(beta-L-fucopyranosyl)oxy]propanimidate
analogue of guanosine 5'-diphospho-beta-L-fucose. 57% inhibition at 0.1 microM
PCMB
-
5 mM, complete inhibition, inhibition can be very significantly prevented by GDP-fucose, GDP or GnGnGp
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
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
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
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
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
alpha(1,6)FT activity is considerably higher in colorectal tumour tissue than in healthy tissue and is related to gender, lymph node metastasis, type of growth and tumour stage
additional information
-
44.1 U/l in HEK-293 cells transfected with epidermal growth factor receptor and FUT8, 1.8 U/l in HEK-293 cells transfected only with epidermal growth factor receptor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 37
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
14 splice variants of the alpha6-fucosyltransferase gene are expressed early in human embryos
-
CD34+ cell, activity of 6FucT increases ahead of, and thereafter concomitantly with, cells expressing the CD41a antigen. When the CD41a+ subpopulation of cells is immunoselected (using anti-CD61 i.e. anti GpIIIa antibodies), its 6FucT activity increases proportionally to the yield of DC61+ cells
-
thrombin-activated neutrophils release cathepsin G and elastase during coagulation of blood, which promotes the degranulation of platelets and hence the secretion of alpha-6-fucosyltransferase
thrombin-activated neutrophils release cathepsin G and elastase during coagulation of blood, which promotes the degranulation of platelets and hence the secretion of alpha-6-fucosyltransferase
-
a significant increase in the alpha(1,6)FT expression in colorectal tumour tissues as compared to healthy and transitional tissues, inflammatory lesions and adenomas is observed
expression in hepatoma tissues and their surrounding tissues and in tissues with chronic disease, overview
enzyme is expressed in hepatoma tissues and their surrounding tissues with chronic disease, but not in normal liver
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Fut8 partially localizes to the cell surface in an SH3-dependent manner
additional information
-
typical type II membrane protein, which is localized in the Golgi apparatus
Fut8 has an Src homology 3 (SH3) domain at the luminal side of the Golgi apparatus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme down-regulation promotes hemoglobin production and erythroid differentiation
physiological function
physiological function
enzyme overexpression inhibits hemoglobin production in erythroleukemia cells
physiological function
FUT8 is the sole enzyme responsible for the N-acetylglucosaminyltransferase GnT I-independent core fucosylation pathway. In a a stable HEK-293S GnT I-/- cell line with either knockdown of FUT8, the erythropoietin produced shows the pure Man5GlcNAc2 glycoform, whereas that produced from the FUT8-overexpressing cell line is fully core-fucosylated oligomannose glycan (Man5GlcNAc2Fuc)
physiological function
FUT8 potentially forms homodimers in vivo via intermolecular hydrophobic interactions involving alpha-helical domains. alpha-Helical and SH3 domains are all required for enzymatic activity. The SH3 domain locates in close proximity to the alpha-helical domain in an intermolecular manner
physiological function
the SH3 domain of Fut8, located at the luminal side of the Golgi apparatus, is essential for FUT8 activity both in cells and in vitro. Residue His535 in the SH3 domain is the critical residue for enzymatic activity of FUT8. Ribophorin I (RPN1), a subunit of the oligosaccharyltransferase complex, is an SH3-dependent binding protein of FUT8. RPN1 knockdown decreases both FUT8 activity and core fucose levels
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). FUT8_HUMAN
575
1
66516
Swiss-Prot
Secretory Pathway (Reliability: 1)
A8K8P8_HUMAN
575
1
66516
TrEMBL
Secretory Pathway (Reliability: 1)
Q546E0_HUMAN
575
1
66516
TrEMBL
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
60000
additional information
additional information
amino acid sequence alignment and comparison of conserved regions, consensus peptide motif
additional information
-
amino acid sequence alignment and comparison of conserved regions, consensus peptide motif
additional information
amino acid sequence alignment and comparison of conserved regions, consensus peptide motif
additional information
hydrophobic cluster analysis, peptide motif regions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
no glycoprotein
no N-glycosylation sites in predicted amino acid sequence
no glycoprotein
no N-glycosylation sites in predicted amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure at 2.6 A resolution
molecular modeling predicts homophilic dimerization. Residues Ala123, Leu130, and Leu137 of alpha1-helix, and Ala149, Leu156, Ile163, Leu170 of the alpha2-helix all contribute to the formation of the hydrophobic core in the four alpha-helices bundle. The bundle is formed via intermolecular and intramolecular hydrophobic interactions and provides an interface for other intermolecular interactions. In the prediction, each of the SH3 domains is located in close proximity to the interface formed by the alpha-helical domain of the counterpart in the predicted dimer
structure of FUT8 complexed with GDP and a biantennary complex N-glycan (G0). FUT8 follows an SN2 mechanism and deploys a series of loops and an alpha-helix which all contribute in forming the binding site. An exosite, formed by one of these loops and an SH3 domain, is responsible for the recognition of branched sugars, making contacts specifically to the alpha-1,3 arm GlcNAc, required for catalysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D32C
mutation introduces covalent dimerization, activity is similar to wild-type
additional information
additional information
-
gene transfection to human hepatoma and mice mutants, overexpression and effects on tumour growth
additional information
gene transfection to human hepatoma and mice mutants, overexpression and effects on tumour growth
additional information
-
293/EGFR/FUT8, HEK-293 cells transfected with epidermal growth factor receptor and FUT8, increased fucosylation of EGFR, about 20% increase of cellular growth in response to epidermal growth factor stiumlation, enhanced cellular sensitivity to gefitinib, decrease of epidermal growth factor-mediated phosphorylation of mitogen-activated protein kinase
additional information
-
293/EGFR/shFUT8, stable knockdown mutant of intrinsic FUT8, about 20% decrease of cellular growth in response to epidermal growth factor stimulation
additional information
-
A549/shFUT8, knockdown mutant of intrinsic FUT8, no enzyme activity, decrease of cellular growth in response to epidermal growth factor stimulation, decreased sensitivity of A549 cells to gefitinib
additional information
the N-terminal alpha-helical domain is required for the full activity. The deletion of residues 1-67 and residues 1-108 has no effect on the activity. Further deletion results in the loss of activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography with GDP-hexanolamine resin and GnGn-bi-Asn-resin
from blood platelets by affinity chromatography with an asialo-agalacto-transferrin-glycopeptide resin
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned from cDNA library of MKN45 cells, DNA sequence determination and analysis
complete genomic organization for the gene and cloning of two retina splice variants. The presence of the 5'-untranslated exon B diminishes the amount of FUT8 transcript and decreases the alpha6-fucosyltransferase activity by two-thirds, as compared to FUT8 transcripts starting with exon A or C
-
expressed in Sf9 insect cells as soluble enzyme lacking the transmembrane region
large-scale production system for recombinant human FUT8, in which the enzyme is produced in soluble form by baculovirus-infected insect cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
serum alpha1-6-fucosylated alpha-fetoprotein is employed for an early diagnosis of patients with hepatoma and hepatic disease
medicine
-
enzyme of blood platelets is a diagnostic marker for the ploidy level of megakaryocytes in thrombocytopenia
medicine
-
the enzyme is a candidate for the earliest marker of megakaryocyte-commitment in cultured hematopoietic stem cells. Such a marker should allow an earlier detection and earlier transplantation of patients own, ex vivo expanded, megakaryocyte progenitors
medicine
the enzymatic product of core alpha1,6-fucosyltransferase plays a major role in a plethora of pathological conditions, e.g. in prognosis of hepatocellular carcinoma and in colon cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Voynow, J.A.; Scanlin, T.F.; Glick, M.C.
A quantitative method for GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha 1-6fucosyltransferase activity with lectin affinity chromatography
Anal. Biochem.
168
367-373
1988
Homo sapiens
Kaminska, J.; Musielak, M.; Nowicka, A.; Wozniewicz, B.; Koscielak, J.
Neutrophils promote the release of alpha-6-fucosyltransferase from blood platelets through the action of cathepsin G and elastase
Biochimie
83
739-742
2001
Homo sapiens
Uozumi, N.; Teshima, T.; Yamamoto, T.; Nishikawa, A.; Gao, Y.E.; Miyoshi, E.; Gao, C.X.; Noda, K.; Islam, K.N.; et al.
A fluorescent assay method for GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1-6fucosyltransferase activity, involving high performance liquid chromatography
J. Biochem.
120
385-392
1996
Homo sapiens, Rattus norvegicus, Sus scrofa
Yanagidani, S.; Uozumi, N.; Ihara, Y.; Miyoshi, E.; Yamaguchi, N.; Taniguchi, N.
Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells
J. Biochem.
121
626-632
1997
Homo sapiens, Homo sapiens (Q9BYC5), Sus scrofa
Breton, C.; Oriol, R.; Imberty, A.
Conserved structural features in eukaryotic and prokaryotic fucosyltransferases
Glycobiology
8
87-94
1998
Azorhizobium caulinodans (Q43966), Bradyrhizobium japonicum (Q45271), Homo sapiens (Q9BYC5), Sus scrofa (P79282)
Kaminska, J.; Glick, M.C.; Koscielak, J.
Purification and characterization of GDP-L-Fuc:N-acetyl beta-D-glucosaminide alpha1->6 fucosyltransferase from human blood platelets
Glycoconjugate J.
15
783-788
1998
Homo sapiens
Miyoshi, E.; Noda, K.; Yamaguchi, Y.; Inoue, S.; Ikeda, Y.; Wang, W.; Ko, J.H.; Uozumi, N.; Li, W.; Taniguchi, N.
The alpha1-6-fucosyltransferase gene and its biological significance
Biochim. Biophys. Acta
1473
9-20
1999
Homo sapiens, Homo sapiens (Q9BYC5), Rattus norvegicus, Sus scrofa, Sus scrofa (P79282)
Kaminska, J.; Wisniewska, A.; Koscielak, J.
Chemical modifications of alpha1,6-fucosyltransferase define amino acid residues of catalytic importance
Biochimie
85
303-310
2003
Homo sapiens
Bany-Laszewicz, U.; Kaminska, J.; Klimczak-Jajor, E.; Koscielak, J.
The activity of alpha1,6-fucosyltransferase during human megakaryocytic differentiation
Cell. Mol. Biol. Lett.
9
145-152
2004
Homo sapiens
Martinez-Duncker, I.; Michalski, J.C.; Bauvy, C.; Candelier, J.J.; Mennesson, B.; Codogno, P.; Oriol, R.; Mollicone, R.
Activity and tissue distribution of splice variants of alpha6-fucosyltransferase in human embryogenesis
Glycobiology
14
13-25
2004
Homo sapiens
Ihara, H.; Ikeda, Y.; Taniguchi, N.
Reaction mechanism and substrate specificity for nucleotide sugar of mammalian alpha1,6-fucosyltransferase--a large-scale preparation and characterization of recombinant human FUT8
Glycobiology
16
333-342
2006
Homo sapiens
Ihara, H.; Ikeda, Y.; Toma, S.; Wang, X.; Suzuki, T.; Gu, J.; Miyoshi, E.; Tsukihara, T.; Honke, K.; Matsumoto, A.; Nakagawa, A.; Taniguchi, N.
Crystal structure of mammalian {alpha}1,6-fucosyltransferase, FUT8
Glycobiology
17
455-466
2007
Homo sapiens (Q9BYC5), Homo sapiens
Muinelo-Romay, L.; Vazquez-Martin, C.; Villar-Portela, S.; Cuevas, E.; Gil-Martin, E.; Fernandez-Briera, A.
Expression and enzyme activity of alpha(1,6)fucosyltransferase in human colorectal cancer
Int. J. Cancer
123
641-646
2008
Homo sapiens
Matsumoto, K.; Shimizu, C.; Arao, T.; Andoh, M.; Katsumata, N.; Kohno, T.; Yonemori, K.; Koizumi, F.; Yokote, H.; Aogi, K.; Tamura, K.; Nishio, K.; Fujiwara, Y.
Identification of predictive biomarkers for response to trastuzumab using plasma FUCA activity and N-glycan identified by MALDI-TOF-MS
J. Proteome Res.
8
457-462
2009
Homo sapiens (Q9BYC5)
Matsumoto, K.; Yokote, H.; Arao, T.; Maegawa, M.; Tanaka, K.; Fujita, Y.; Shimizu, C.; Hanafusa, T.; Fujiwara, Y.; Nishio, K.
N-Glycan fucosylation of epidermal growth factor receptor modulates receptor activity and sensitivity to epidermal growth factor receptor tyrosine kinase inhibitor
Cancer Sci.
99
1611-1617
2008
Homo sapiens
Koetzler, M.P.; Blank, S.; Bantleon, F.I.; Spillner, E.; Meyer, B.
Donor substrate binding and enzymatic mechanism of human core alpha1,6-fucosyltransferase (FUT8)
Biochim. Biophys. Acta
1820
1915-1925
2012
Homo sapiens (Q9BYC5)
Muinelo-Romay, L.; Villar-Portela, S.; Cuevas, E.; Gil-Martin, E.; Fernandez-Briera, A.
Identification of alpha(1,6)fucosylated proteins differentially expressed in human colorectal cancer
BMC Cancer
11
508
2011
Homo sapiens
Ihara, H.; Hanashima, S.; Okada, T.; Ito, R.; Yamaguchi, Y.; Taniguchi, N.; Ikeda, Y.
Fucosylation of chitooligosaccharides by human alpha1,6-fucosyltransferase requires a nonreducing terminal chitotriose unit as a minimal structure
Glycobiology
20
1021-1033
2010
Homo sapiens
Sasaki, H.; Toda, T.; Furukawa, T.; Mawatari, Y.; Takaesu, R.; Shimizu, M.; Wada, R.; Kato, D.; Utsugi, T.; Ohtsu, M.; Murakami, Y.
alpha-1,6-Fucosyltransferase (FUT8) inhibits hemoglobin production during differentiation of murine and K562 human erythroleukemia cells
J. Biol. Chem.
288
16839-16847
2013
Homo sapiens (Q9BYC5), Mus musculus (Q9WTS2)
Ihara, H.; Okada, T.; Taniguchi, N.; Ikeda, Y.
Involvement of the alpha-helical and Src homology 3 domains in the molecular assembly and enzymatic activity of human alpha1,6-fucosyltransferase, FUT8
Biochim. Biophys. Acta
1864
129596
2020
Homo sapiens (Q9BYC5)
Manabe, Y.; Kasahara, S.; Takakura, Y.; Yang, X.; Takamatsu, S.; Kamada, Y.; Miyoshi, E.; Yoshidome, D.; Fukase, K.
Development of alpha1,6-fucosyltransferase inhibitors through the diversity-oriented syntheses of GDP-fucose mimics using the coupling between alkyne and sulfonyl azide
Bioorg. Med. Chem.
25
2844-2850
2017
Homo sapiens (Q9BYC5)
Yang, Q.; Wang, L.X.
Mammalian alpha-1,6-fucosyltransferase (FUT8) is the sole enzyme responsible for the N-acetylglucosaminyltransferase I-independent core fucosylation of high-mannose N-glycans
J. Biol. Chem.
291
11064-11071
2016
Homo sapiens (Q9BYC5)
Yang, Q.; Zhang, R.; Cai, H.; Wang, L.X.
Revisiting the substrate specificity of mammalian alpha1,6-fucosyltransferase reveals that it catalyzes core fucosylation of N-glycans lacking alpha1,3-arm GlcNAc
J. Biol. Chem.
292
14796-14803
2017
Homo sapiens (Q9BYC5)
Tomida, S.; Takata, M.; Hirata, T.; Nagae, M.; Nakano, M.; Kizuka, Y.
The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation
J. Biol. Chem.
295
7992-8004
2020
Homo sapiens (Q9BYC5)
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