3'(2'),5'-bisphosphate nucleotidase

From Wikipedia, the free encyclopedia

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 $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 3.1.3.7
BRENDA references for 3.1.3.7 (Recommended.)
PubMed references for 3.1.3.7
PubMed Central references for 3.1.3.7
Google Scholar references for 3.1.3.7
Brungraber EG (1958). "Nucleotides involved in the enzymatic conjugation of phenols with sulfate". J. Biol. Chem. 233: 472–477.
Farooqui AA, Balasubramanian AS (1970). "Enzymatic dephosphorylation 3'-phosphoadenosine 5'-phoaphosulfate to adenosine 5'-phosphosulfate in sheep brain". Biochim. Biophys. Acta. 198: 56–65. PMID 4313079.
Ramaswamy SG, Jakoby WB (1987). "(2')3',5'-Bisphosphate nucleotidase". J. Biol. Chem. 262: 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: 113–21. doi:10.1111/j.1432-1033.1976.tb10395.x. PMID 179817.