EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   5.1.3.7 | more |
the deficiency in UDP-N-acetylglucosamine 4-epimerase accounts for all glycosylation defects observed in lslD cells, including production of abnormal LDL receptors |
Cricetulus griseus |
? |
- |
? |
| 5.1.3.7 | more |
UDP-N-acetylglucosamine 4-epimerase increases during spherulation, a process that involves the synthesis of galactosamine walls |
Physarum polycephalum |
? |
- |
? |
| 5.1.3.7 | more |
the enzyme plays an important role in the outer coat synthesis in the later sporulation stage |
Priestia megaterium |
? |
- |
? |
| 5.1.3.7 | more |
enzyme regulates gastric mucous aminosugar metabolism |
Rattus norvegicus |
? |
- |
? |
| 5.1.3.7 | more |
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 |
Bacillus anthracis |
? |
- |
? |
| 5.1.3.7 | more |
Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-D-glucose to UDP-D-galactose and between their N-acetylated forms |
Thermus thermophilus |
? |
- |
? |
| 5.1.3.7 | more |
the enzyme is active on both acetylated and non-acetylated UDP-hexoses, see for EC 5.1.3.2 |
Marinithermus hydrothermalis |
? |
- |
? |
| 5.1.3.7 | more |
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 |
Thermotoga maritima |
? |
- |
? |
| 5.1.3.7 | more |
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 |
Escherichia coli |
? |
- |
? |
| 5.1.3.7 | more |
the group 3 epimerase WbpP from Pseudomonas aeruginosa is very specific for N-acetylated substrates |
Pseudomonas aeruginosa |
? |
- |
? |
