3'(2'),5'-bisphosphate nucleotidase
| 3'(2'),5'-bisphosphate nucleotidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 3'(2'),5'-bisphosphate nucleotidase monomer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 3.1.3.7 | ||||||||
| CAS no. | 9025-83-6 | ||||||||
| 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 3'(2'),5'-bisphosphate nucleotidase (EC 3.1.3.7) is an enzyme that catalyzes the chemical reaction
- adenosine 3',5'-bisphosphate + H2O adenosine 5'-phosphate + phosphate
Thus, the two substrates of this enzyme are adenosine 3',5'-bisphosphate and H2O, whereas its two products are adenosine 5'-phosphate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is adenosine-3'(2'),5'-bisphosphate 3'(2')-phosphohydrolase. Other names in common use include phosphoadenylate 3'-nucleotidase, 3'-phosphoadenylylsulfate 3'-phosphatase, phosphoadenylate 3'-nucleotidase, and 3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase. This enzyme participates in sulfur metabolism.
Structural studies[]
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1JP4, 1K9Y, 1K9Z, 1KA0, 1KA1, and 1QGX.
References[]
- Brungraber EG (1958). "Nucleotides involved in the enzymatic conjugation of phenols with sulfate". J. Biol. Chem. 233 (2): 472–477. PMID 13563523.
- Farooqui AA, Balasubramanian AS (1970). "Enzymatic dephosphorylation 3'-phosphoadenosine 5'-phoaphosulfate to adenosine 5'-phosphosulfate in sheep brain". Biochim. Biophys. Acta. 198 (1): 56–65. doi:10.1016/0005-2744(70)90032-x. PMID 4313079.
- Ramaswamy SG, Jakoby WB (1987). "(2')3',5'-Bisphosphate nucleotidase". J. Biol. Chem. 262 (21): 10044–7. PMID 3038862.
- Lik-Shing Tsang M, Schiff JA (1976). "Properties of enzyme fraction A from Chlorella and copurification of 3' (2'), 5'-biphosphonucleoside 3' (2')-phosphohydrolase, adenosine 5'phosphosulfate sulfohydrolase and adenosine-5'-phosphosulfate cyclase activities". Eur. J. Biochem. 65 (1): 113–21. doi:10.1111/j.1432-1033.1976.tb10395.x. PMID 179817.
- EC 3.1.3
- Enzymes of known structure
- EC 3.1 stubs