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Literature summary for 3.6.1.13 extracted from
- The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family (2001), Nat. Struct. Biol., 8, 467-472.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapor diffusion at 18°C. The structure of the apo enzyme, the active enzyme and the complex with ADP-ribose are determined to 1.9 A, 2.7 A and 2.3 A, respectively. The Nudix motif residues, folded as a loop-helix-loop tailored for diphosphate hydrolysis, compose the catalytic center | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | Q93K97 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADPribose + H2O | - |
Escherichia coli | AMP + D-ribose 5-phosphate | - |
? |  |
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Release 2023.1 (January 2023)
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