EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.335 | expression in Escherichia coli | Pseudomonas aeruginosa |
1.1.1.335 | expression in Escherichia coli | Thermus thermophilus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.335 | crystal structure of the enzyme in a complex with NAD(H), to 1.5 A resolution. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft | Pseudomonas aeruginosa |
1.1.1.335 | crystal structures of the enzyme in a complex with NAD(H) and 2-oxoglutarate, and the enzyme in a complex with NAD(H) and its substrate UDP-N-acetyl-D-glucosaminuronic acid, to 1.45 A and 2.0 A resolution, respectively. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft. Residues Lys101 and His185 most likely play key roles in catalysis | Thermus thermophilus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.335 | Pseudomonas aeruginosa | G3XD23 | - |
- |
1.1.1.335 | Thermus thermophilus | Q72KX8 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.335 | WblA | - |
Pseudomonas aeruginosa |
1.1.1.335 | WblA | - |
Thermus thermophilus |