2.4.1.65 D112E muation decreases activity of the enzyme and does not interfere with H-type 1/H-type 2 acceptors 637646 2.4.1.65 D125E site-directed mutagenesis of FucT-V, the mutant activity is similar to the wild-type enzyme activity 693000 2.4.1.65 D336A fucosyltransferase III mutant enzyme shows reduced activity with a variety of acceptors, 40fold reduction in activity for Fucalpha(1,2)Galbeta(1,3)GlcNAc. 4fold reduction affinity for GDP-fucose. 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 637645 2.4.1.65 E111D site-directed mutagenesis of FucT-VI, the mutant activity is similar to the wild-type enzyme activity 693000 2.4.1.65 FT3dc mutant where the cytoplasmic domain (Asp-2 to Trp-13) is deleted 661236 2.4.1.65 I126V site-directed mutagenesis of FucT-V, the mutant activity is similar to the wild-type enzyme activity 693000 2.4.1.65 K73T site-directed mutagenesis of FucT-VI, the mutant shows increased activity compared to the wild-type enzyme 693000 2.4.1.65 K73T/E111D site-directed mutagenesis of FucT-VI, the mutant shows increased activity compared to the wild-type enzyme 693000 2.4.1.65 K73T/I75V/T87A insertion mutagenesis of FucT-VI, the mutant shows altered substrate specificity compared to the wild-type enzyme 693000 2.4.1.65 K73T/R110W site-directed mutagenesis of FucT-VI, the mutant shows increased activity compared to the wild-type enzyme 693000 2.4.1.65 K73T/R110W/E111D/V112I site-directed mutagenesis of FucT-VI, the mutant shows increased activity compared to the wild-type enzyme 693000 2.4.1.65 K97S site-directed mutagenesis of FucT-VI, the mutant activity is similar to the wild-type enzyme activity 693000 2.4.1.65 additional information construction of several chimeric mutants by domain swappig, overview 693000 2.4.1.65 additional information with full length UA948FucT, only 20% of total enzyme activities are 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 UA948(1-371) has little enzyme activity. UA948(10-434) and UA948(1-434) completely lose activity -, 680736 2.4.1.65 R110H less than 10% of the wild type alpha-1,3-activity and undetectable alpha-1,4-activity 661839 2.4.1.65 R110K less than 10% of the wild type alpha-1,3-activity and undetectable alpha-1,4-activity 661839 2.4.1.65 R110N less than 10% of the wild type alpha-1,3-activity and undetectable alpha-1,4-activity 661839 2.4.1.65 R110Q less than 10% of the wild type alpha-1,3-activity and undetectable alpha-1,4-activity 661839 2.4.1.65 R110Q naturally occurring missense mutation in the FUT7 gene, the mutation abolishes FUT7 enzyme activity and synthesis of E-selectin binding ligands on leukocytes, and increases the expression of FUT4, the mutant shows unaltered synthesis of P-selectin binding ligand, overview 662567 2.4.1.65 R110W no alpha-1,3-activity or alpha-1,4-activity 661839 2.4.1.65 R110W site-directed mutagenesis of FucT-VI, the mutant shows increased activity compared to the wild-type enzyme 693000 2.4.1.65 R110W/E111D/V112I site-directed mutagenesis of FucT-VI, the mutant shows increased activity compared to the wild-type enzyme 693000 2.4.1.65 R96S site-directed mutagenesis of FucT-VI, the mutant activity is similar to the wild-type enzyme activity 693000 2.4.1.65 S110R site-directed mutagenesis of FucT-V, the mutant activity is similar to the wild-type enzyme activity 693000 2.4.1.65 S111K site-directed mutagenesis of FucT-V, the mutant activity is similar to the wild-type enzyme activity 693000 2.4.1.65 T87K site-directed mutagenesis of FucT-V, the mutant shows decreased activity compared to the wild-type enzyme 693000 2.4.1.65 T87K/D125E site-directed mutagenesis of FucT-V, the mutant shows decreased activity compared to the wild-type enzyme 693000 2.4.1.65 T87K/V89I/A101T insertion mutagenesis of FucT-V, the mutant shows altered substrate specificity compared to the wild-type enzyme 693000 2.4.1.65 T87K/W124R site-directed mutagenesis of FucT-V, the mutant shows decreased activity compared to the wild-type enzyme 693000 2.4.1.65 T87K/W124R/D125E/I126V site-directed mutagenesis of FucT-V, the mutant shows decreased activity compared to the wild-type enzyme 693000 2.4.1.65 V112I site-directed mutagenesis of FucT-VI, the mutant activity is similar to the wild-type enzyme activity 693000 2.4.1.65 W111A alpha-1,4-activity is decreased to 10-20% of the wild type activity 661839 2.4.1.65 W111F alpha-1,4-activity is decreased to 42% of the wild type activity 661839 2.4.1.65 W111R the mutation changes the specificity for fucose transfer from H-type 1 to H-type 2 acceptors 637646 2.4.1.65 W111Y alpha-1,4-activity is decreased to 58% of the wild type activity 661839 2.4.1.65 W11R/D112E the mutation changes the specificity for fucose transfer from H-type 1 to H-type 2 acceptors. Increased type 2 activity compared to mutant W111R 637646 2.4.1.65 W124A alpha-1,4-activity is decreased to 20% of the wild type activity 661839 2.4.1.65 W124F alpha-1,4-activity is decreased to 17% of the wild type activity 661839 2.4.1.65 W124R site-directed mutagenesis of FucT-V, the mutant shows decreased activity compared to the wild-type enzyme 693000 2.4.1.65 W124R undetectable alpha-1,4-activity 661839 2.4.1.65 W124R/D125E/I126V site-directed mutagenesis of FucT-V, the mutant shows decreased activity compared to the wild-type enzyme 693000 2.4.1.65 W124V undetectable alpha-1,4-activity 661839 2.4.1.65 W124Y alpha-1,4-activity is decreased to 52% of the wild type activity 661839