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

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 2 ADP
bis(5'-nucleosyl)-tetraphosphatase (symmetrical)
Identifiers
EC number3.6.1.41
CAS number85638-48-8
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 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.

Structural studies

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

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References
    • Barnes LD, Culver CA (1982). "Isolation and characterization of diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase from Physarum polycephalum". Biochemistry. 21 (24): 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 (24): 14784–9. PMID 6317672.


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