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Information on EC 2.4.1.214 - glycoprotein 3-alpha-L-fucosyltransferase and Organism(s) Helicobacter pylori and UniProt Accession O30511
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2.4.1.214 glycoprotein 3-alpha-L-fucosyltransferaseIUBMB Comments
Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-alpha-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-beta-L-fucose to form an alpha1,3-linkage rather than an alpha1,6-linkage. The {iupac/misc/glycp#3.5::N-glycan} products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).
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Word Map
- 2.4.1.214
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lewis
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sialylated
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fucosylated
- selectins
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p-selectin
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fucts
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alpha1,3-fucosylated
- psgl-1
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fuc-tiv
- ligand-1
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alpha1,3fucosyltransferases
- n-acetyllactosamine
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polylactosamine
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sialyl-lewis
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alpha2,3-sialylated
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anti-horseradish
- beta1,2-xylosyltransferase
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selectin-dependent
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skin-homing
- lacto-n-neotetraose
- st3gal
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alpha2,3-sialyltransferase
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counterreceptors
- lacto-n-tetraose
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sialyl-lex
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lewis-type
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meca-79
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alpha1,3-fucose
- fuct-iii
- alpha1,3/4-fucosyltransferases
- synthesis
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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=
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+
Synonyms
fuct-vii, fuc-tvii, alpha1,3-fucosyltransferase, fuct-iv, fucosyltransferase vii, fut11, fucta, alpha(1,3)fucosyltransferase, alpha3-fucosyltransferase, fuct vii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtFUT11
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-
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core alpha-(1,3)-fucosyltransferase
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-
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Fuc-T C3
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-
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FucT1
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-
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FucTA
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-
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GDP-fucose:beta-N-acetylglucosamine (Fuc to (Fuca1-6GlcNAc)-Asn-peptide) alpha1-3-fucosyltransferase
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GDP-L-fuc:Asn-linked GlcNAc alpha1,3-fucosyltransferase
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GDP-L-fuc:N-acetyl-beta-D-glucosaminide alpha1,3-fucosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
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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) 3-alpha-L-fucosyl-transferase
Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-alpha-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-beta-L-fucose to form an alpha1,3-linkage rather than an alpha1,6-linkage. The {iupac/misc/glycp#3.5::N-glycan} products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).
CAS REGISTRY NUMBER
COMMENTARY
68247-53-0
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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-fucose + N-acetyllactosamine
GDP + 3-fucosyl-N-acetyllactosamine
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-
-
?
GDP-fucose + N-acetyllactosamine
GDP + Galbeta1-4(Fucalpha1-3)GlcNAc
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FucT involved in production of the Lewis x trisaccharide, the major component of the bacterias lipopolysaccharides
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0683
GDP-fucose
deletion mutant FTdelta23 with 23 residues deleted from the C-terminus
0.07864
GDP-fucose
deletion mutant FTdelta66 with 66 residues deleted from the C-terminus
0.07967
GDP-fucose
deletion mutant FTdelta38 with 38 residues deleted from the C-terminus
0.08831
GDP-fucose
deletion mutant FTdelta45 with 45 residues deleted from the C-terminus
0.09356
GDP-fucose
deletion mutant FTdelta28 with 28 residues deleted from the C-terminus
0.09864
GDP-fucose
deletion mutant FTdelta80 with 80 residues deleted from the C-terminus
0.228
GDP-fucose
deletion mutant FTdelta115 with 115 residues deleted from the C-terminus
0.7
LacNAc
deletion mutant FTdelta38 with 38 residues deleted from the C-terminus
0.71
LacNAc
deletion mutant FTdelta45 with 45 residues deleted from the C-terminus
0.71
LacNAc
deletion mutant FTdelta66 with 66 residues deleted from the C-terminus
0.78
LacNAc
deletion mutant FTdelta23 with 23 residues deleted from the C-terminus
0.78
LacNAc
deletion mutant FTdelta28 with 28 residues deleted from the C-terminus
0.89
LacNAc
deletion mutant FTdelta80 with 80 residues deleted from the C-terminus
8.92
LacNAc
deletion mutant FTdelta115 with 115 residues deleted from the C-terminus
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00059
GDP-N-(biphenyl-4-ylmethyl)-5-(1H-1,2,3-triazol-1-yl)pentanamide
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.38
deletion mutant FTdelta115 with 115 residues deleted from the C-terminus, substrate LacNAc
2.52
deletion mutant FTdelta23 with 23 residues deleted from the C-terminus, substrate LacNAc
4.84
deletion mutant FTdelta28 with 28 residues deleted from the C-terminus, substrate LacNAc
5.04
deletion mutant FTdelta38 with 38 residues deleted from the C-terminus, substrate LacNAc
5.2
deletion mutant FTdelta80 with 80 residues deleted from the C-terminus, substrate LacNAc
5.72
deletion mutant FTdelta45 with 45 residues deleted from the C-terminus, substrate LacNAc
5.82
deletion mutant FTdelta66 with 66 residues deleted from the C-terminus, substrate LacNAc
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by the hanging drop vapor diffusion method, as FucT, FucT-GDPfucose and FucT-GDP complexes
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
structural analysis of the FT of Helicobacter pylori by systematic C-terminal truncation reveals that up to 80 residues, including the region rich in hydrophobic and positively charged residues (434-478) and 5 of the 10 tandem repeats of 7 amino acids each (399-433) can be removed without significant change in structure and catalysis, half of the heptad repeats required to maintain both the secondary and native quaternary structures, systematic deletion of the C-terminus considerably improves the solubility of the protein, truncated forms are highly specific for type 2 sugar substrates that contain the Galbeta-1,4-GlcNAc structure, type 1 substrate Galbeta-1,3-GlcNAc is not accepted
additional information
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structural analysis of the FT of Helicobacter pylori by systematic C-terminal truncation reveals that up to 80 residues, including the region rich in hydrophobic and positively charged residues (434-478) and 5 of the 10 tandem repeats of 7 amino acids each (399-433) can be removed without significant change in structure and catalysis, half of the heptad repeats required to maintain both the secondary and native quaternary structures, systematic deletion of the C-terminus considerably improves the solubility of the protein, truncated forms are highly specific for type 2 sugar substrates that contain the Galbeta-1,4-GlcNAc structure, type 1 substrate Galbeta-1,3-GlcNAc is not accepted
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression Escherichia coli to obtain a selenomethionine-labeled L202M FucT for crystallization
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lin, S.W.; Yuan, T.M.; Li, J.R.; Lin, C.H.
Carboxyl terminus of Helicobacter pylori alpha1,3-fucosyltransferase determines the structure and stability
Biochemistry
45
8108-8116
2006
Helicobacter pylori (O30511), Helicobacter pylori
Sun, H.Y.; Lin, S.W.; Ko, T.P.; Pan, J.F.; Liu, C.L.; Lin, C.N.; Wang, A.H.; Lin, C.H.
Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design
J. Biol. Chem.
282
9973-9982
2007
Helicobacter pylori, Helicobacter pylori NCTC11639
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