In
enzymology, a
bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) is an
enzyme that
catalyzes the
chemical reaction- P1,P4-bis(5'-guanosyl) tetraphosphate + H2O GTP + GMP
Thus, the two substrates of this enzyme are P1,P4-bis(5'-guanosyl) tetraphosphate and H2O, whereas its two products are GTP and GMP.
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 nucleotidohydrolase. Other names in common use include bis(5'-guanosyl)-tetraphosphatase, bis(5'-adenosyl)-tetraphosphatase, diguanosinetetraphosphatase (asymmetrical), dinucleosidetetraphosphatase (asymmetrical), diadenosine P1,P4-tetraphosphatase, dinucleoside tetraphosphatase, and 1-P,4-P-bis(5'-nucleosyl)-tetraphosphate nucleotidohydrolase. This enzyme participates in purine metabolism and pyrimidine metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
- Jakubowski H, Guranowski A "Enzymes hydrolyzing ApppA and/or AppppA in higher plants Purification and some properties of diadenosine triphosphatase, diadenosine tetraphosphatase, and phosphodiesterase from yellow lupin (Lupinus luteus) seeds". J. Biol. Chem. 258 9982–9.
- Vallejo CG, Lobaton CD, Quintanilla M, Sillero A, Sillero MA "Dinucleosidasetetraphosphatase in rat liver and Artemia salina". Biochim. Biophys. Acta. 438 304–9.
- Warner AH, Finamore FJ "Isolation, purification, and characterization of P1,P4-diguanosine 5'-tetraphosphate asymmetrical-pyrophosphohydrolase from brine shrimp eggs". Biochemistry. 4 1568–75.
External links
- The CAS registry number for this enzyme class is .
Gene Ontology (GO) codes