The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori
Marta Bošnjaković
; Division of Physical Chemistry, Ruđer Bošković Institute, POB 180, HR-10002 Zagreb, Croatia
Ivana Leščić Ašler
; Division of Physical Chemistry, Ruđer Bošković Institute, POB 180, HR-10002 Zagreb, Croatia
Zoran Štefanić
orcid.org/0000-0002-3486-4291
; Division of Physical Chemistry, Ruđer Bošković Institute, POB 180, HR-10002 Zagreb, Croatia
APA 6th Edition Bošnjaković, M., Leščić Ašler, I. i Štefanić, Z. (2018). The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori. Croatica Chemica Acta, 91 (2), 171-175. https://doi.org/10.5562/cca3335
MLA 8th Edition Bošnjaković, Marta, et al. "The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori." Croatica Chemica Acta, vol. 91, br. 2, 2018, str. 171-175. https://doi.org/10.5562/cca3335. Citirano 26.02.2021.
Chicago 17th Edition Bošnjaković, Marta, Ivana Leščić Ašler i Zoran Štefanić. "The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori." Croatica Chemica Acta 91, br. 2 (2018): 171-175. https://doi.org/10.5562/cca3335
Harvard Bošnjaković, M., Leščić Ašler, I., i Štefanić, Z. (2018). 'The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori', Croatica Chemica Acta, 91(2), str. 171-175. https://doi.org/10.5562/cca3335
Vancouver Bošnjaković M, Leščić Ašler I, Štefanić Z. The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori. Croatica Chemica Acta [Internet]. 2018 [pristupljeno 26.02.2021.];91(2):171-175. https://doi.org/10.5562/cca3335
IEEE M. Bošnjaković, I. Leščić Ašler i Z. Štefanić, "The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori", Croatica Chemica Acta, vol.91, br. 2, str. 171-175, 2018. [Online]. https://doi.org/10.5562/cca3335
Sažetak Purine nucleoside phosphorylase (PNP) is an essential enzyme in the purine salvage pathway of Helicobacter pylori. Since H. pylori lacks the ability to synthesize purine nucleosides de novo, inhibition of this enzyme could stop the growth of this bacterium. However, for the design of successful inhibitors the details of the mechanism of this enzyme should be fully understood. PNPs catalyze cleavage of the glycosidic bond of purine nucleosides, and phosphate is one of the substrates. It is thought that binding of phosphate induces the conformational change as a necessary initial step in the catalysis. This conformational change is manifested in closing of either one of the six active sites in the homohexameric PNPs. It is unclear whether the binding of phosphate is sufficient or just a necessary condition for the closing of the active site. In this paper we conducted an experiment to check this by soaking the crystals of the apo form of the enzyme in increasing concentrations of phosphate.