Bis(5'-nucleosyl)-tetraphosphatase (symmetrical)

From Wikipedia, the free encyclopedia

In enzymology, a bis(5'-nucleosyl)-tetraphosphatase (symmetrical) (EC 3.6.1.41) is an enzyme that catalyzes the chemical reaction

P₁,P₄-bis(5'-adenosyl) tetraphosphate + H₂O $\rightleftharpoons$ 2 ADP

Thus, the two substrates of this enzyme are P1,P4-bis(5'-adenosyl) tetraphosphate and H₂O, whereas its product is ADP.

This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is P1,P4-bis(5'-nucleosyl)-tetraphosphate nucleosidebisphosphohydrolase. Other names in common use include diadenosinetetraphosphatase (symmetrical), dinucleosidetetraphosphatasee (symmetrical), symmetrical diadenosine tetraphosphate hydrolase, adenosine tetraphosphate phosphodiesterase, Ap4A hydrolase, bis(5'-adenosyl) tetraphosphatase, diadenosine tetraphosphate hydrolase, diadenosine polyphosphate hydrolase, diadenosine 5',5-P1,P4-tetraphosphatase, diadenosinetetraphosphatase (symmetrical), 1-P,4-P-bis(5'-nucleosyl)-tetraphosphate, and nucleosidebisphosphohydrolase. This enzyme participates in purine metabolism.

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

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2DFJ and 2QJC.

[edit] References

IUBMB entry for 3.6.1.41
BRENDA references for 3.6.1.41 (Recommended.)
PubMed references for 3.6.1.41
PubMed Central references for 3.6.1.41
Google Scholar references for 3.6.1.41
Barnes LD, Culver CA (1982). "Isolation and characterization of diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase from Physarum polycephalum". Biochemistry. 21: 6123–8. doi:10.1021/bi00267a015. PMID 6295456.
Guranowski A, Jakubowski H, Holler E (1983). "Catabolism of diadenosine 5',5"'-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5',5"'-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12". J. Biol. Chem. 258: 14784–9. PMID 6317672.