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
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme 3′(2′),5′-bisphosphate nucleotidase (EC 3.1.3.7) catalyzes several related reactions. For example, when characterised from guinea pig liver and Debaryomyces hansenii, it hydrolyses adenosine 3',5'-bisphosphat to adenosine monophosphate and orthophosphate:[1][2]

 
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 

It also hydrolyses 3'-phosphoadenosine-5'-phosphosulfate to 5'-adenylyl sulfate, which has a role in the incorporation of sulfate in metabolism.[3][4][5]

 
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q356138.
5'-adenylyl sulfate

This enzyme is a hydrolase, specifically one 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.[6]

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1JP4​, PDB: 1K9Y​, PDB: 1K9Z​, PDB: 1KA0​, PDB: 1KA1​, and PDB: 1QGX​.

References

  1. ↑ 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.
  2. ↑ Aggarwal, Monika; Bansal, Parmil K.; Mondal, Alok K. (2005). "Molecular cloning and biochemical characterization of a 3′(2′),5′-bisphosphate nucleotidase from Debaryomyces hansenii". Yeast. 22 (6): 457–470. doi:10.1002/yea.1223. PMID 15849794.
  3. ↑ Farooqui AA, Balasubramanian AS (1970). "Enzymatic dephosphorylation 3′-phosphoadenosine 5′-phosphosulfate to adenosine 5′-phosphosulfate in sheep brain". Biochim. Biophys. Acta. 198 (1): 56–65. doi:10.1016/0005-2744(70)90032-x. PMID 4313079.
  4. ↑ 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.
  5. ↑ Hudson, Benjamin H.; York, John D. (2012). "Roles for nucleotide phosphatases in sulfate assimilation and skeletal disease". Advances in Biological Regulation. 52 (1): 229–238. doi:10.1016/j.advenzreg.2011.11.002. PMC 3845023. PMID 22100882.
  6. ↑ Enzyme 3.1.3.7 at KEGG Pathway Database.