dGTPase
| dGTPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.5.1 | ||||||||
| CAS no. | 9025-63-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme dGTPase (EC 3.1.5.1)[1][2] catalyzes the reaction
- dGTP + H2O deoxyguanosine + triphosphate
This enzyme belongs to the family of hydrolases, specifically those acting on triphosphoric monoester bonds. The systematic name is dGTP triphosphohydrolase. Other names in common use include deoxy-GTPase, deoxyguanosine 5-triphosphate triphosphohydrolase, deoxyguanosine triphosphatase, and deoxyguanosine triphosphate triphosphohydrolase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1HA3, 2C77, 2C78, and 2DQB.
References
- ^ Kornberg SR, Lehman IR, Bessman MJ, Simms ES, Kornberg A (1958). "Enzymatic cleavage of deoxyguanosine triphosphate to deoxyguanosine and tripolyphosphate". J. Biol. Chem. 233 (1): 159–62. doi:10.1016/S0021-9258(19)68047-6. PMID 13563461.
- ^ Seto D, Bhatnagar SK, Bessman MJ (1988). "The purification and properties of deoxyguanosine triphosphate triphosphohydrolase from E. coli". J. Biol. Chem. 263 (3): 1494–99. doi:10.1016/S0021-9258(19)57330-6. PMID 2826481.