DGTPase
Enzyme
dGTPase | |||||||||
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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 | ||||||||
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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. 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.
- v
- t
- e
ester hydrolases
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Protein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Protein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
Phosphodiesterase
deoxyribonuclease
and ribonuclease)
3.1.11-16: Exonuclease |
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3.1.21-31: Endonuclease |
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