dGTPase
| dGTPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.5.1 | ||||||||
| CAS number | 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 / EGO | ||||||||
| |||||||||
In enzymology, a dGTPase (EC 3.1.5.1) is an enzyme that catalyzes the chemical reaction
- dGTP + H2O deoxyguanosine + triphosphate
Thus, the two substrates of this enzyme are dGTP and H2O, whereas its two products are deoxyguanosine and triphosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on triphosphoric monoester bonds. The systematic name of this enzyme class 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. 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. PMID 2826481.
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