This is an abbreviated version! For detailed information about 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase, go to the full flat file.
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
synthesis of fluorescein-isothiocyanate-labeled and carboxyfluorescein-labeled NDP-beta-L-fucose derivatives, and application in labeling of different glycoproteins with the aid of fucosyltransferases. The fluorescein-isothiocyanate-labeled fucose is the best of these substrates, and the bacterial enzyme FucT tolerates the fluorescent substrates better than human fucosyltransferases
synthesis of fluorescein-isothiocyanate-labeled and carboxyfluorescein-labeled NDP-beta-L-fucose derivatives, and application in labeling of different glycoproteins with the aid of fucosyltransferases. The fluorescein-isothiocyanate-labeled fucose is the best of these substrates, and the bacterial enzyme FucT tolerates the fluorescent substrates better than human fucosyltransferases
development of a high-throughput screening system for identification of FucT-VII inhibitors, which could have anti-inflammatory or anti-metastatic potential, utilizing scintillation proximity assay with fetuin-coated beads, overview
FT-IV and FT-VII are both important contributors to selectin-dependent eosinophil recruitment to the skin and may represent therapeutic targets in which eosinophil recruitment contributes to pathophysiology
granzyme B-induced caspase 3-activation leads to up-regulation of FUT4 and FUT9 mRNA expression, which increases the surface expression of Lewis X and Y antigens
fucosyltransferase IV overexpression promotes cell proliferation, increases the expression of proliferating cell nuclear antigen and augments Lewis Y expression to trigger neoplastic cell proliferation, fucosyltransferase IV may serve as a potential therapeutic target for the treatment of Lewis Y-positive epithelial cancers
recombinant yeast cells which provide an inexpensive, self-perpetuating source of fucosyltransferase activity immobilized in the cell wall, useful for in vitro synthesis of sLex
stable expression of beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans and human FucT9 in CHO cells, producing fucosylated poly-LacdiNAc N-glycans
a KO line lacking two XylT genes and four FucT genes expressing a human IgG2 antibody shows an IgG2 expression level as high as in a control transformant. The IgG glycosylation profile shows no beta(1,2)-xylose or alpha(1,3)-fucose present on the glycosylation moiety. The dominant glycoform is the GnGn structure
expression of bacterial alpha-1,3-fucosyltransferase in engineered Escherichia coli deficient in beta-galactosidase activity and expressing the essential enzymes for the production of guanosine 5'-diphosphate-L-fucose, for synthesis of 3-fucosyllactose. The fucT gene gives the best 3-fucosyllactose production in a simple batch fermentation process using glycerol as a carbon source and lactose as an acceptor. With concomitant blocking the colanic acid biosynthetic pathway, the recombinant strain exhibits the highest concentration (11.5 g/l), yield (0.39 mol/mol), and productivity (0.22 g/l/h) of 3-fucosyllactose in glycerol-limited fed-batch fermentation
to overcome the poor solubility of FutA upon expression in Escherichia coli, codon optimization, and systematic truncation of the protein at the C-terminus with only one heptad repeat remaining yield 150-200 mg/l of soluble protein of FutA and result in more than an 18fold increase in the 3-fucosyllactose yield. Mutant A128N obtained by focused directed evolution mutant displays a 3.4fold higher catalytic activity than wild-type FutA. Mutant A128N/H129E/Y132I exhibits a 9.6fold improvement in specific activity when compared to wild-type. Mutants A128N/H129E/S46F and A128N/H129E/Y132I/S46F show synergistic effects, that is 14.5- and 15.5fold improvement in specific activity relative to wild-type. The mutations increase the binding affinity for lactose and kcat values for lactose and GDP-fucose. The quadruple mutant A128N/H129E/Y132I/S46F synthesizes 3-fucosyllactose with an improved yield and productivity (more than 96% yield based on 5 mM of GDP-Fuc within 1 h)
to overcome the poor solubility of FutA upon expression in Escherichia coli, codon optimization, and systematic truncation of the protein at the C-terminus with only one heptad repeat remaining yield 150-200 mg/l of soluble protein of FutA and result in more than an 18fold increase in the 3-fucosyllactose yield. Mutant A128N obtained by focused directed evolution mutant displays a 3.4fold higher catalytic activity than wild-type FutA. Mutant A128N/H129E/Y132I exhibits a 9.6fold improvement in specific activity when compared to wild-type. Mutants A128N/H129E/S46F and A128N/H129E/Y132I/S46F show synergistic effects, that is 14.5- and 15.5fold improvement in specific activity relative to wild-type. The mutations increase the binding affinity for lactose and kcat values for lactose and GDP-fucose. The quadruple mutant A128N/H129E/Y132I/S46F synthesizes 3-fucosyllactose with an improved yield and productivity (more than 96% yield based on 5 mM of GDP-Fuc within 1 h)