| adenosine-tetraphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.1.14 | ||||||||
| CAS no. | 37289-26-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an adenosine-tetraphosphatase (EC 3.6.1.14) is an enzyme that catalyzes the chemical reaction
- adenosine 5'-tetraphosphate + H2O ATP + phosphate
Thus, the two substrates of this enzyme are adenosine 5'-tetraphosphate and H2O, whereas its two products are ATP and phosphate.
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 adenosine-tetraphosphate phosphohydrolase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2V7Q.
References
- Small GD, Cooper C (1966). "Purification and properties of nucleoside tetraphosphate hydrolase from rabbit muscle". Biochemistry. 5 (1): 14–26. doi:10.1021/bi00865a003. PMID 4287215.
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