Bis(5'-nucleosyl)-tetraphosphatase (symmetrical)
bis(5'-nucleosyl)-tetraphosphatase (symmetrical) | |||||||||
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Identifiers | |||||||||
EC no. | 3.6.1.41 | ||||||||
CAS no. | 85638-48-8 | ||||||||
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 | ||||||||
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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
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
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2DFJ and 2QJC.
References
[edit]- 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. doi:10.1016/S0021-9258(17)43729-X. PMID 6317672.