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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
Search PMC articles PubMed articles NCBI proteins

The enzyme 3′(2′),5′-bisphosphate nucleotidase (EC 3.1.3.7) catalyzes the reaction

adenosine 3′,5′-bisphosphate + H₂O ${\displaystyle \rightleftharpoons }$ AMP + phosphate

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is adenosine-3′(2′),5′-bisphosphate 3′(2′)-phosphohydrolase. Other names in common use include phosphoadenylate 3′-nucleotidase, 3′-phosphoadenylylsulfate 3′-phosphatase, 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. doi:10.1016/S0021-9258(18)64786-6. 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. doi:10.1016/S0021-9258(18)61072-5. 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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