CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.79 | Nucleoside Triphosphate Pyrophosphohydrolase |
|
3.90.79.10 | Nucleoside Triphosphate Pyrophosphohydrolase |
Domain Context
CATH Clusters
| Superfamily | Nucleoside Triphosphate Pyrophosphohydrolase |
| Functional Family | ADP-sugar pyrophosphatase isoform X1 |
Enzyme Information
| 3.6.1.13 |
ADP-ribose diphosphatase.
based on mapping to UniProt Q9UKK9
ADP-D-ribose + H(2)O = AMP + D-ribose 5-phosphate.
|
| 3.6.1.58 |
8-oxo-dGDP phosphatase.
based on mapping to UniProt Q9UKK9
8-oxo-dGDP + H(2)O = 8-oxo-dGMP + phosphate.
-!- The enzyme catalyzes the hydrolysis of both 8-oxo-dGDP and 8-oxo-GDP thereby preventing translational errors caused by oxidative damage. -!- The preferred in vivo substrate is not known. -!- The enzyme does not degrade 8-oxo-dGTP and 8-oxo-GTP to the monophosphates (cf. EC 3.6.1.55). -!- Ribonucleotide diphosphates and deoxyribonucleotide diphosphates are hydrolyzed with broad specificity. -!- The bifunctional enzyme NUDT5 also hydrolyzes ADP-ribose to AMP and D-ribose 5-phosphate (cf. EC 3.6.1.13). -!- The human enzyme NUDT18 also hydrolyzes 8-oxo-dADP and 2-hydroxy- dADP, the latter at a slower rate.
|
| 2.7.7.96 |
ADP-D-ribose pyrophosphorylase.
based on mapping to UniProt Q9UKK9
ATP + D-ribose 5-phosphate = diphosphate + ADP-D-ribose.
-!- The human enzyme produces ATP in nuclei in situations of high energy demand, such as chromatin remodeling. -!- The reaction is dependent on the presence of diphosphate. -!- In its absence the enzyme catalyzes the reaction of EC 3.6.1.13. -!- Cf. EC 2.7.7.35.
|
UniProtKB Entries (1)
| Q9UKK9 |
NUDT5_HUMAN
Homo sapiens
ADP-sugar pyrophosphatase
|
PDB Structure
| PDB | 2DSD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structures of Human NUDT5 Reveal Insights into the Structural Basis of the Substrate Specificity
J.Mol.Biol.
|
