Bis(5'-adenosyl)-triphosphatase
| bis(5'-adenosyl)-triphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.1.29 | ||||||||
| CAS no. | 63951-94-0 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a bis(5'-adenosyl)-triphosphatase (EC 3.6.1.29) is an enzyme that catalyzes the chemical reaction
- P1,P3-bis(5'-adenosyl) triphosphate + H2O ADP + AMP
Thus, the two substrates of this enzyme are P1,P3-bis(5'-adenosyl) triphosphate and H2O, whereas its two products are ADP and AMP.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is P1,P3-bis(5'-adenosyl)-triphosphate adenylohydrolase. Other names in common use include dinucleosidetriphosphatase, diadenosine 5,5-P1,P3-triphosphatase, and 1-P,3-P-bis(5'-adenosyl)-triphosphate adenylohydrolase. This enzyme participates metabolic pathways involved in purine metabolism, and may have a role in the development of small cell lung cancer, and non-small cell lung cancer.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1FHI, PDB: 2FHI, PDB: 4FIT, PDB: 5FIT, and PDB: 6FIT.
References
- Jakubowski H, Guranowski A (1983). "Enzymes hydrolyzing ApppA and/or AppppA in higher plants Purification and some properties of diadenosine triphosphatase, diadenosine tetraphosphatase, and phosphodiesterase from yellow lupin (Lupinus luteus) seeds". J. Biol. Chem. 258 (16): 9982–9. doi:10.1016/S0021-9258(17)44594-7. PMID 6309793.
- A; Villalba, R; Moreno, A; Quintanilla, M; Lobatón, CD; Sillero, A (1977). "Dinucleosidetriphosphatase from rat liver. Purification and properties". Eur. J. Biochem. 76 (2): 331–7. doi:10.1111/j.1432-1033.1977.tb11600.x. PMID 196848.