Purine nucleoside phosphorylase DeoD-type (PNP (DeoD-type), PNP)

Purine nucleoside phosphorylase DeoD-type is a **bacterial enzyme**, exemplified in species like *Escherichia coli* and *Bacillus anthracis*, that catalyzes the reversible phosphorolysis of the N-glycosidic bond in beta-(deoxy)ribonucleosides, producing corresponding purine bases and pentose-1-phosphate[2][3][5]. It functions in the **purine salvage pathway**, is hexameric (with multiple active sites per dimer), and is critical for bacterial nucleoside metabolism and survival[3]. Differences between bacterial and human PNP enable its use in **antibacterial drug development** and **experimental cancer therapies** leveraging prodrug activation by the bacterial enzyme[3][4]. Alternative names include **Inosine phosphorylase** and PNP; the gene encoding it in *E. coli* is **deoD**[2]. This enzyme is specific for guanosine, inosine, and adenosine, and its activity is crucial for nucleotide turnover and DNA repair pathways in bacteria[2][3][5][7].

Other names

Inosine phosphorylase2.4.2.1pupdeoD

Enzyme inhibition (for inhibitors: blockade of purine metabolism by suppressing phosphorolysis of nucleosides) - Enzyme-mediated prodrug activation (in gene therapy, bacterial PNP converts prodrugs to toxic metabolites in tumor cells[3])