engleski

Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori

Microaerophilic bacterium Helicobacer pylori is a well known human pathogen involved in the devel-opment of many diseases. Due to the evergrowing infection rate and increase of H. pylori antibioticresistence, it is of utmost importance to find a new way to attack and eradicate H. pylori. The purinemetabolism in H. pylori is solely dependant on the salvage pathway and one of the key enzymes in thispathway is purine nucleoside phosphorylase (PNP). In this timely context, we report here the basic bio-chemical and structural characterization of recombinant PNP from the H. pylori clinical isolate expressedin Escherichia coli. Structure of H. pylori PNP is typical for high molecular mass PNPs. However, its activitytowards adenosine is very low, thus resembling more that of low molecular mass PNPs. Understandingthe molecular mechanism of this key enzyme may lead to the development of new drug strategies andhelp in the eradication of H. pylori.

Helicobacter pylori ; Purine nucleoside phosphorylase ; Purification ; Stability ; Substrate specificity ; Crystal structure

nije evidentirano