2.4.1.152: 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase
This is an abbreviated version!
For detailed information about 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.152
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2.4.1.152
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sialylated
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fucosylated
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selectins
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fuc-tiii
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n-acetyllactosamine
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medicine
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synthesis
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alpha1,3-fucosylation
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lewisx
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fuc-ts
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fuct-iv
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alpha-2-l-fucosyltransferase
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analysis
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drug development
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biotechnology
- 2.4.1.152
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sialylated
-
fucosylated
- selectins
- fuc-tiii
- n-acetyllactosamine
- medicine
- synthesis
-
alpha1,3-fucosylation
- lewisx
- fuc-ts
- fuct-iv
- alpha-2-l-fucosyltransferase
- analysis
- drug development
- biotechnology
Reaction
Synonyms
11639FucT, alpha (1,3) fucosyltransferase, alpha (1,3)-fucosyltransferase, alpha 1,3 fucosyltransferase, alpha 1,3/4 fucosyltransferase Lewis 2, alpha 3-fucosyltransferase IX, alpha(1,3)-fucosyltransferase VII, alpha(1,3)fucosyltransferase IV, alpha(1,3)fucosyltransferase VII, alpha(1-3)fucosyltransferase, alpha-(1,3)-fucosyltransferase, alpha-(1,3)-fucosyltransferase 11, alpha-(1,3)-fucosyltransferase IXa, alpha-(1,3/1,4)-fucosyltransferase, alpha-(1,3/1,4)-FucT, alpha-1,3 FucT-VII, alpha-1,3-fucosyltransferase, alpha-1,3-fucosyltransferase 3, alpha-1,3-fucosyltransferase 9D, alpha-1,3-fucosyltransferase VI, alpha-1,3-FucT3, alpha-13-fucosyltransferase VII, alpha-3-fucosyltransferase, alpha-3-L-fucosyltransferase, alpha1,3 fucosyltransferase, alpha1,3 fucosyltransferase VII, alpha1,3 FucT-VII, alpha1,3-fucosyltransferase, alpha1,3-fucosyltransferase 4, alpha1,3-fucosyltransferase 9, alpha1,3-fucosyltransferase C, alpha1,3-fucosyltransferase IX, alpha1,3-fucosyltransferase V, alpha1,3-fucosyltransferase VI, alpha1,3-fucosyltransferase-F, alpha1,3-FucT, alpha1,3-FucTIX, alpha1,3/4-fucosyltransferase, alpha1,3/4-fucosyltransferase VI, alpha1,3FT, alpha1,3fucosyltransferase-VII, alpha1-3 fucosyltransferase, alpha1-3 fucosyltransferase-VII, alpha1-3 FucT, alpha1->3fucosyltransferase, alpha3-fucosyltransferase, alpha3-fucosyltransferase IX, alpha3-fucosyltransferase VII, alpha3-fucosyltransferase-V, alpha3-fucosyltransferase-VI, alpha3/4FucT, CEFT-3, CEFT-4, FT-IV, FT-VII, Fuc-Tb, Fuc-TV, Fuc-TXI, fucosyltransferase, fucosyltransferase 11, fucosyltransferase 4, fucosyltransferase 7, fucosyltransferase IV, fucosyltransferase IX, fucosyltransferase V, fucosyltransferase VI, fucosyltransferase VII, fucosyltransferase, guanosine diphosphofucose-glucoside alpha1-->3-, fucosyltransferase-7, fucosyltransferase-VII, fucosyltransferaseIX, FucT, FucT 9, FucT IX, FucT V, FucT-IX, FucT-VI, FucT-VII, FucT-XI, FucT7, FucT9, FucTC, FucTD, FucTe, FucTVII, FUT VI, FuT-F, FUT-VI, FUT10, FUT11, FUT3, FUT4, FUT5, FUT6, FUT7, Fut9, FUT9a, FutA, FutB, galactoside 3-fucosyltransferase, galactoside 3-L-fucosyltransferase 11, GDL-L-fucose:N-acetyl-beta-D-glucosaminyl alpha-3-L-fucosyltransferase, GDP-Fuc:Galbeta1-4GlcNAc (Fuc to GlcNAc) alpha1-3 fucosyltransferase, GDP-fucose:beta-D-N-acetylglucosaminide 3-alpha-fucosyltransferase, GDP-fucose:Galbeta(1-4)GlcNAc-R alpha(1-3)fucosyltransferase, GDP-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-galactosaminyl-R 3-L-fucosyltransferase, guanosine diphosphofucose glucoside alpha1->3fucosyltransferase, HP_0379, HP_0651, Lewis type alpha1,3-FucT, lewis-negative alpha-3-fucosyltransferase, LEwis-type alpha1,3-fucosyltransferase, Lj4g3v0598850, More, plasma alpha-3-fucosyltransferase, PylT, rat fucosyltransferase VII, rFuc-TVII, rFUT7, sFUT9, UA948FucT, WP-000487420, WP-000487428, WP-000487430, XM_016585847, zebrafisha1-3fucosyltrasferase 1, zFT1
ECTree
2.4.1.152 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.152 - 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A128N
A128N/H129E
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the mutant displays 6.5fold higher catalytic activity with D-lactose than the wild type enzyme
A128N
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mutant obtained by focused directed evolution mutant, 3.4fold higher catalytic activity than wild-type
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A349D
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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
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mutant enzyme is inactive, mutant enzyme produces a series of lower molecular weight bands when characterized by Wester blot and does not bind GDP
N101Q
N101Q/N153Q
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the mutations lead to an almost complete loss of enzymatic activity
N153Q
N62Q
N62Q/N101Q
N62Q/N153Q
additional information
A128N
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the mutant displays 3.4fold higher catalytic activity with D-lactose than the wild type enzyme
A128N
mutant obtained by focused directed evolution mutant, 3.4fold higher catalytic activity than wild-type
N62Q/N101Q
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the mutations lead to an almost complete loss of enzymatic activity
N62Q/N153Q
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the mutations lead to an almost complete loss of enzymatic activity
additional information
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with full length 11639FucT, 28% of total enzyme activities is localized in the soluble fraction. For alpha-(1,3/1,4)-fucosyltransferase(1441), this increases to 45%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. Truncation mutant alpha-(1,3/1,4)-fucosyltransferase(10447) completely loses activity
additional information
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with full length UA948FucT, 20% of total enzyme activities is localized in the soluble fraction. For UA948(1-428), this increases to 47%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. UA948(1-364), a mutant with the entire heptad repeat region removed, exhibits extremely low levels of enzyme activity. This indicates that the heptad repeat region is essential for enzyme activity. Construct alpha-(1,3/1,4)-fucosyltransferase(1-371) has little enzyme activity. alpha-(1,3/1,4)-fucosyltransferase(10-434) and alpha-(1,3/1,4)-fucosyltransferase(1-434) completely lose activity
additional information
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
additional information
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
additional information
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
additional information
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
additional information
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
additional information
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
additional information
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
additional information
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
additional information
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
additional information
-
the C-terminus of FutB is composed of 7 heptad repeats, construction of truncated forms, with C-terminal deletions of 25, 43, 57, and 78 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type. Deletion of half the membrane-anchoring region in the variant lacking 25 amino acids does not improve 3-fucosyllactose production. Truncation of 78 amino acids decreases the production of 3-fucosyllactose
-
additional information
-
wild-type C-terminus contains two heptad repeats. Construction of truncated forms, with C-terminal deletions of 27, 46, 53, and 59 residues. Upon expression in Escherichia coli, the truncated proteins show enhanced expression levels, i.e. 7fold for the shortest variant. Cells expressing the truncation variant lacking 43 amino acids produce 4.7 times more 3-fucosyllactose compared to wild-type
-
additional information
-
the C-terminus of PylT is composed of 10 heptad repeats, responsible for dimerization of the enzymes, and a peripheral membrane anchoring region. Upon deletion of the 42-amino acid-long membrane-binding region, 3-fucosyllactose production by the recombinant enzyme is improved by 4.5fold
-
additional information
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with full length 11639FucT, 28% of total enzyme activities is localized in the soluble fraction. For alpha-(1,3/1,4)-fucosyltransferase(1441), this increases to 45%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. Truncation mutant alpha-(1,3/1,4)-fucosyltransferase(10447) completely loses activity
-
additional information
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with full length UA948FucT, 20% of total enzyme activities is localized in the soluble fraction. For UA948(1-428), this increases to 47%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. UA948(1-364), a mutant with the entire heptad repeat region removed, exhibits extremely low levels of enzyme activity. This indicates that the heptad repeat region is essential for enzyme activity. Construct alpha-(1,3/1,4)-fucosyltransferase(1-371) has little enzyme activity. alpha-(1,3/1,4)-fucosyltransferase(10-434) and alpha-(1,3/1,4)-fucosyltransferase(1-434) completely lose activity
-
additional information
-
with full length 11639FucT, 28% of total enzyme activities is localized in the soluble fraction. For alpha-(1,3/1,4)-fucosyltransferase(1441), this increases to 45%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. Truncation mutant alpha-(1,3/1,4)-fucosyltransferase(10447) completely loses activity
-
additional information
-
with full length UA948FucT, 20% of total enzyme activities is localized in the soluble fraction. For UA948(1-428), this increases to 47%, respectively, indicating that truncation of the C-terminal putative alpha-helices increases FucT solubility. UA948(1-364), a mutant with the entire heptad repeat region removed, exhibits extremely low levels of enzyme activity. This indicates that the heptad repeat region is essential for enzyme activity. Construct alpha-(1,3/1,4)-fucosyltransferase(1-371) has little enzyme activity. alpha-(1,3/1,4)-fucosyltransferase(10-434) and alpha-(1,3/1,4)-fucosyltransferase(1-434) completely lose activity
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additional information
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catalytic domain of alpha-1,3-fucosyltransferase (amino acids 37-441) are expressed in Saccharomyces cerevisiae and Pichia pastoris as a fusion protein HSP150 delta-FucTe consisting of HSP150delta (1-321) and catalytic domain of FucTe (37-441) to promote proper folding and secretion
additional information
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Saccharomyces cerevisiae strain created co-expressing the catalytic domain of alpha-2,3-sialyltransferase and Fuc-Te in the cell wall, addition of N-acetyllactosamine, CMP-sialic acid and GDP-fucose results in the production of sLex
additional information
construction of mutants FUT9dcyt, FUT9d6, FUT9S/A, subcellular localization analysis of recombinant FUT9wt and mutants in HeLa cells
additional information
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construction of mutants FUT9dcyt, FUT9d6, FUT9S/A, subcellular localization analysis of recombinant FUT9wt and mutants in HeLa cells
additional information
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deletion of the -2,067 to -662 nt region enhances luciferase activity. The FUT VI promoter regions carrying deletions of conserved binding motifs are unaffected by overexpression of Oct-1 via transfection with pcDNA3.2/Oct--1
additional information
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a marked reduction in formation of metastatic foci is observed in FucT7 deficient mice injected with murine colon carcinoma cells MC-38GFP
additional information
double knock-out mice deficient for both FT-IV and FT-VII show an essential absence of eosinophil recruitment to the dermis
additional information
double knock-out mice deficient for both FT-IV and FT-VII show an essential absence of eosinophil recruitment to the dermis
additional information
FT-IV deficient mice show a significant decrease in eosinophil recruitment to the skin
additional information
FT-IV deficient mice show a significant decrease in eosinophil recruitment to the skin
additional information
FT-VII deficient mice show a decrease in eosinophil recruitment to the skin
additional information
FT-VII deficient mice show a decrease in eosinophil recruitment to the skin
additional information
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O-linked oligosaccharides attached to GlyCAM-1 are analyzed in FucT-VII deficient mice, an 80% reduction in alpha1,3-fucosylated structures in 6-sulfo sialyl Lewis X and a significant increase in 6-sulfo N-acetyllactosamine are found in high-endothelial venules in secondary lymphoid organs of FucT-VII -/- mice, surprisingly, the amount of 6-sulfated galactose (Gal) is also increased in mutant mice, since 6-sulfo galactose can be synthesized by keratin sulfate sulfotransferase (KSST) it could be concluded that FucT-VII and KSST may compete for the same acceptor molecules
additional information
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primary adhesion of Th1 lymphocytes obtained from FucT-VII deficient mice is drastically reduced
