5'-acylphosphoadenosine hydrolase
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| 5'-acylphosphoadenosine hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.1.20 | ||||||||
| CAS no. | 37289-31-9 | ||||||||
| 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, a 5'-acylphosphoadenosine hydrolase (EC 3.6.1.20) is an enzyme that catalyzes the chemical reaction
- 5'-acylphosphoadenosine + H2O AMP + a carboxylate
Thus, the two substrates of this enzyme are 5'-acylphosphoadenosine and H2O, whereas its two products are AMP and carboxylate.
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 5'-acylphosphoadenosine acylhydrolase. This enzyme is also called 5-phosphoadenosine hydrolase. This enzyme participates in purine metabolism.
References
- Kellerman GM (May 1959). "Isolation and characteristics of the enzyme acyl 5'-nucleotidase". Biochimica et Biophysica Acta. 33 (1): 101–5. doi:10.1016/0006-3002(59)90502-5. PMID 13651188.
