From Wikipedia, the free encyclopedia
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
Search
PMC articles
PubMed articles
NCBI proteins

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

  1. ^ 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.
  2. ^ 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.


From Wikipedia, the free encyclopedia
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
Search
PMC articles
PubMed articles
NCBI proteins

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

  1. ^ 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.
  2. ^ 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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