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UDP-alpha-D-galactose
UDP-alpha-D-glucose
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-D-glucose
UDP-D-galactose
UDP-glucose
UDP-galactose
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-alpha-D-glucosamine
epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
UDP-N-acetylglucosamine
UDP-N-acetylgalactosamine
-
-
-
r
additional information
?
-
UDP-D-glucose

UDP-D-galactose
-
-
-
-
r
UDP-D-glucose
UDP-D-galactose
-
the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
-
-
r
UDP-D-glucose
UDP-D-galactose
-
-
-
-
r
UDP-D-glucose
UDP-D-galactose
-
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
-
r
UDP-D-glucose
UDP-D-galactose
-
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
-
-
r
UDP-GlcNAc

UDP-GalNAc
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
-
-
-
r
UDP-glucose

UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine

UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-D-glucosamine

UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
r
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
r
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
r
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
equilibrium reaction resulting in a 70:30 ratio of UDP-GlcNAc to UDP-GalNAc, irrespective of the initial substrate
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
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
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
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-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
-
-
r
UDP-N-acetylgalactosamine

UDP-N-acetylglucosamine
Q81JK4
-
-
-
r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
-
GalE epimerizes UDP-N-acetylgalactosamine in a dose-dependent manner
-
-
r
additional information

?
-
Q81JK4
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme is active on both acetylated and non-acetylated UDP-hexoses, see for EC 5.1.3.2
-
-
?
additional information
?
-
-
UDP-N-acetylglucosamine 4-epimerase increases during spherulation, a process that involves the synthesis of galactosamine walls
-
-
?
additional information
?
-
-
the enzyme plays an important role in the outer coat synthesis in the later sporulation stage
-
-
?
additional information
?
-
the group 3 epimerase WbpP from Pseudomonas aeruginosa is very specific for N-acetylated substrates
-
-
?
additional information
?
-
-
enzyme regulates gastric mucous aminosugar metabolism
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-D-glucose
UDP-D-galactose
-
the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
-
-
r
UDP-glucose
UDP-galactose
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
UDP-N-acetylglucosamine
UDP-N-acetylgalactosamine
-
-
-
r
additional information
?
-
UDP-N-acetyl-alpha-D-glucosamine

UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
-
-
-
r
UDP-N-acetyl-D-glucosamine

UDP-N-acetyl-D-galactosamine
-
the enzyme provides Gal and galNAc residues for the synthesis of the cell-surface carbohydrates in Campylobacter jejuni NCTC 11168
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-galactosamine
-
the enzyme is responsible for the presence of N-acetylgalactosamine in the exopolysaccharide repeating units of both strains, LY03 and Sfi20
-
?
UDP-N-acetylgalactosamine

UDP-N-acetylglucosamine
Q81JK4
-
-
-
r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
-
GalE epimerizes UDP-N-acetylgalactosamine in a dose-dependent manner
-
-
r
additional information

?
-
Q81JK4
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
UDP-N-acetylglucosamine 4-epimerase increases during spherulation, a process that involves the synthesis of galactosamine walls
-
-
?
additional information
?
-
-
the enzyme plays an important role in the outer coat synthesis in the later sporulation stage
-
-
?
additional information
?
-
-
enzyme regulates gastric mucous aminosugar metabolism
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.