| 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.
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Adenosine triphosphate
Transcription
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.
This page was last edited on 26 August 2023, at 12:58