5.1.3.7 additional information the deficiency in UDP-N-acetylglucosamine 4-epimerase accounts for all glycosylation defects observed in lslD cells, including production of abnormal LDL receptors ? - ? 89 5.1.3.7 additional information UDP-N-acetylglucosamine 4-epimerase increases during spherulation, a process that involves the synthesis of galactosamine walls ? - ? 89 5.1.3.7 additional information the enzyme plays an important role in the outer coat synthesis in the later sporulation stage ? - ? 89 5.1.3.7 additional information enzyme regulates gastric mucous aminosugar metabolism ? - ? 89 5.1.3.7 additional information the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase ? - ? 89 5.1.3.7 additional information Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-D-glucose to UDP-D-galactose and between their N-acetylated forms ? - ? 89 5.1.3.7 additional information the enzyme is active on both acetylated and non-acetylated UDP-hexoses, see for EC 5.1.3.2 ? - ? 89 5.1.3.7 additional information enzyme TMGalE also has high activity for epimerization of UDP-Gal to UDP-Glc, EC 5.1.3.2. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively ? - ? 89 5.1.3.7 additional information substrate specificity of KfoA, overview. KfoA epimerizes both acetylated and non-acetylated (UDP-Glc) substrates, EC 5.1.3.2, but its kcat/Km value for UDP-GlcNAc is approximately 1300fold that for UDP-Glc. Recombinant KfoA showes a strong preference for acetylated substrates in vitro. Coupling of K4 chondroitin polymerase (KfoC) and KfoA to determine the activity of UDP-GlcNAc 4-epimerase ? - ? 89 5.1.3.7 additional information the group 3 epimerase WbpP from Pseudomonas aeruginosa is very specific for N-acetylated substrates ? - ? 89 5.1.3.7 additional information two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, EC 5.1.3.2, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates ? - ? 89 5.1.3.7 UDP-alpha-D-galactose - UDP-alpha-D-glucose - r 424154 5.1.3.7 UDP-alpha-D-glucose epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose UDP-alpha-D-galactose - r 368620 5.1.3.7 UDP-D-glucose - UDP-D-galactose - r 368624 5.1.3.7 UDP-D-glucose the achieved reasonable conversion rates the amount of enzyme used is increased 200fold comparted to UDP-N-acetyl-D-glucosamine as substrate. Substrate conversions reach 20% for UDP-Glc and 65% for UDP-Gal UDP-D-galactose - r 368624 5.1.3.7 UDP-D-glucose the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168 UDP-D-galactose - r 368624 5.1.3.7 UDP-D-glucose unlike the wild-type enzyme the mutant enzyme is more efficient in catalyzing the reaction with the non-acetylated hexoses UDP-Glc and UDP-Gal than in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine UDP-D-galactose - r 368624 5.1.3.7 UDP-GlcNAc - UDP-GalNAc - r 368622 5.1.3.7 UDP-glucose - UDP-galactose - r 444422 5.1.3.7 UDP-N-acetyl-alpha-D-galactosamine epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose UDP-N-acetyl-alpha-D-glucosamine - r 445966 5.1.3.7 UDP-N-acetyl-alpha-D-glucosamine - UDP-N-acetyl-alpha-D-galactosamine - ? 427565 5.1.3.7 UDP-N-acetyl-alpha-D-glucosamine - UDP-N-acetyl-alpha-D-galactosamine - r 427565 5.1.3.7 UDP-N-acetyl-alpha-D-glucosamine epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose UDP-N-acetyl-alpha-D-galactosamine - r 427565 5.1.3.7 UDP-N-acetyl-D-glucosamine - UDP-N-acetyl-D-galactosamine - ? 966 5.1.3.7 UDP-N-acetyl-D-glucosamine - UDP-N-acetyl-D-galactosamine - r 966 5.1.3.7 UDP-N-acetyl-D-glucosamine r UDP-N-acetyl-D-galactosamine - ? 966 5.1.3.7 UDP-N-acetyl-D-glucosamine equilibrium reaction resulting in a 70:30 ratio of UDP-GlcNAc to UDP-GalNAc, irrespective of the initial substrate UDP-N-acetyl-D-galactosamine - r 966 5.1.3.7 UDP-N-acetyl-D-glucosamine the enzyme is responsible for the presence of N-acetylgalactosamine in the exopolysaccharide repeating units of both strains, LY03 and Sfi20 UDP-N-acetyl-D-galactosamine - ? 966 5.1.3.7 UDP-N-acetyl-D-glucosamine the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168 UDP-N-acetyl-D-galactosamine - r 966 5.1.3.7 UDP-N-acetyl-D-glucosamine wild-type enzyme is more efficient in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine than in catalyzing the epimerization of UDP-glucose and UDP-galactose UDP-N-acetyl-D-galactosamine - r 966 5.1.3.7 UDP-N-acetylgalactosamine - UDP-N-acetylglucosamine - r 407447 5.1.3.7 UDP-N-acetylgalactosamine GalE epimerizes UDP-N-acetylgalactosamine in a dose-dependent manner UDP-N-acetylglucosamine - r 407447 5.1.3.7 UDP-N-acetylglucosamine - UDP-N-acetylgalactosamine - r 386755