2.4.1.68: glycoprotein 6-alpha-L-fucosyltransferase
This is an abbreviated version!
For detailed information about glycoprotein 6-alpha-L-fucosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.68
Reaction
Synonyms
6FucT, alfC, alpha(1,6)FT, alpha(1,6)fucosyltransferase, alpha-1,6-fucosyltransferase, alpha-6-fucosyltransferase, alpha1,6-fucosyltransferase, alpha1,6-FucT, alpha1,6FucT, alpha1-6,fucosyltransferase, alpha1-6FucT, alpha6FucT, BN194_28780, fucosyltransferase 8, fucosyltransferase, guanosine diphosphofucose-glycoprotein, FUT8, GDP-fucose glycoprotein fucosyltransferase, GDP-fucose-glycoprotein fucosyltransferase, GDP-L-fuc:N-acetyl-beta-D-glucosaminide alpha1-6fucosyltransferase, GDP-L-fucose-glycoprotein fucosyltransferase, GDP-L-fucose:2-acetamido-2-deoxy-beta-D-glucoside 6-alpha-L-fucosyltransferase, GDPfucose glycoprotein fucosyltransferase, glycoprotein fucosyltransferase, guanosine diphosphofucose-glycoprotein fucosyltransferase, NodZ, NodZ fucosyltransferase
ECTree
2.4.1.68 glycoprotein 6-alpha-L-fucosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.68 - glycoprotein 6-alpha-L-fucosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N183/341Q
the mutant shows reduced activity compared to the wild type enzyme
N183D
the mutant shows reduced activity compared to the wild type enzyme
N183D/N341D
the mutant shows reduced activity compared to the wild type enzyme
N341D
the mutant shows reduced activity compared to the wild type enzyme
N341Q
the mutant shows reduced activity compared to the wild type enzyme
D32C
mutation introduces covalent dimerization, activity is similar to wild-type
D200A
-
mutation at the nucleophilic residue, does not provide a typical glycosynthase activity
E274A
-
mutation at the general acid/base residue, mutant acts as efficient glycoligase able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins
E274G
-
mutation at the general acid/base residue, mutant acts as efficient glycoligase able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins
E274S
-
mutation at the general acid/base residue, mutant acts as efficient glycoligase able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins
D200A
-
mutation at the nucleophilic residue, does not provide a typical glycosynthase activity
-
E274A
-
mutation at the general acid/base residue, mutant acts as efficient glycoligase able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins
-
E274G
-
mutation at the general acid/base residue, mutant acts as efficient glycoligase able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins
-
E274S
-
mutation at the general acid/base residue, mutant acts as efficient glycoligase able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins
-
additional information
additional information
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knockdown mutant by constitutive expression of short-hairpin RNA against FuT8
additional information
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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
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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
