CATH Classification

Domain Context

CATH Clusters

Superfamily Nucleoside Triphosphate Pyrophosphohydrolase
Functional Family ADP-sugar pyrophosphatase

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 2DSB
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
Zha, M., Zhong, C., Peng, Y., Hu, H., Ding, J.
J.Mol.Biol.