CATH Classification

Domain Context

CATH Clusters

Superfamily Nucleoside Triphosphate Pyrophosphohydrolase
Functional Family 7,8-dihydro-8-oxoguanine triphosphatase

Enzyme Information

3.6.1.56
2-hydroxy-dATP diphosphatase.
based on mapping to UniProt P36639
2-hydroxy-dATP + H(2)O = 2-hydroxy-dAMP + diphosphate.
-!- The enzyme hydrolyzes oxidized purine nucleoside triphosphates such as 2-hydroxy-dATP, thereby preventing their misincorporation into DNA. -!- It can also recognize 8-oxo-dGTP and 8-oxo-dATP, but with lower efficiency (cf. EC 3.6.1.55).
3.6.1.55
8-oxo-dGTP diphosphatase.
based on mapping to UniProt P36639
8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate.
-!- This enzyme hydrolyzes the phosphoanhydride bond between the alpha and beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA. -!- It does not hydrolyze 2-hydroxy-dATP (cf. EC 3.6.1.56).

UniProtKB Entries (1)

P36639
8ODP_HUMAN
Homo sapiens
7,8-dihydro-8-oxoguanine triphosphatase

PDB Structure

PDB 5NHY
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Novel Class of Potent and Cellularly Active Inhibitors Devalidates MTH1 as Broad-Spectrum Cancer Target.
Ellermann, M., Eheim, A., Rahm, F., Viklund, J., Guenther, J., Andersson, M., Ericsson, U., Forsblom, R., Ginman, T., Lindstrom, J., Silvander, C., Tresaugues, L., Giese, A., Bunse, S., Neuhaus, R., Weiske, J., Quanz, M., Glasauer, A., Nowak-Reppel, K., Bader, B., Irlbacher, H., Meyer, H., Queisser, N., Bauser, M., Haegebarth, A., Gorjanacz, M.
ACS Chem. Biol.