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

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
3'(2'),5'-bisphosphate nucleotidase
Identifiers
EC number3.1.3.7
CAS number9025-83-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

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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.


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