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The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori


Bošnjaković, Marta; Leščić Ašler, Ivana; Štefanić, Zoran
The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori // Croatica chemica acta, 91 (2018), 2; 171-175 doi:10.5562/cca3335 (međunarodna recenzija, članak, znanstveni)


Naslov
The Role of Phosphate Binding in Purine Nucleoside Phosphorylase of Helicobacter pylori

Autori
Bošnjaković, Marta ; Leščić Ašler, Ivana ; Štefanić, Zoran

Izvornik
Croatica chemica acta (0011-1643) 91 (2018), 2; 171-175

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Active site conformation, enzyme catalysis, purine nucleoside phosphorylase, phosphate binding

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.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija



POVEZANOST RADA


Projekt / tema
HRZZ-IP-2013-11-7423 - Enzimi purinskog reciklirajućeg ciklusa iz Helicobacter pylori i Escherichie coli (Marija Luić, )

Ustanove
Institut "Ruđer Bošković", Zagreb

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus


Uključenost u ostale bibliografske baze podataka:


  • CAPlus
  • DOAJ
  • EBSCO – Academic Search Complete
  • HRČAK
  • ProQuest


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