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Literature summary for 3.6.1.13 extracted from
- Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase (2002), Biochemistry, 41, 9279-9285.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | dependent on | 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 | nucleophilic attack at the adenosyl phosphate. The enzyme cycles between an open free enzyme and a closed substrate-metal complex conformation. This cycling may be important in preventing nonspecific hydrolysis of other nucleotides | Escherichia coli | AMP + D-ribose 5-phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADP-ribose pyrophosphatase | - |
Escherichia coli |
| ADPRase | - |
Escherichia coli |
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