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Uridine phosphorylase (UP) is a key enzyme of pyrimidine salvage pathways that enables the recycling of endogenous or exogenous-supplied pyrimidines and plays an important intracellular metabolic role. Here, we biochemically and structurally characterized two evolutionarily divergent uridine phosphorylases, PcUP1 and PcUP2 from the oomycete pathogen  Phytophthora capsici . Our analysis of other oomycete genomes revealed that both uridine phosphorylases are present in  Phytophthora  and  Pythium  genomes, but only  UP2  is seen in  Saprolegnia spp . which are basal members of the oomycetes. Moreover, uridine phosphorylases are not found in obligate oomycete pathogens such as  Hyaloperonospora arabidopsidis  and  Albugo spp. PcUP 1 and  PcUP2  are upregulated 300 and 500 fold respectively, within 90 min after infection of pepper leaves. The crystal structures of PcUP1 in ligand-free and in complex with uracil/ribose-1-phosphate, 2′-deoxyuridine/phosphate and thymidine/phosphate were analyzed. Crystal structure of this uridine phosphorylase showed strict conservation of key residues in the binding pocket. Structure analysis of PcUP1 with bound ligands, and site-directed mutagenesis of key residues provide additional support for the “push-pull” model of catalysis. Our study highlights the importance of pyrimidine salvage during the earliest stages of infection.

Structural and catalytic analysis of two diverse uridine phosphorylases in Phytophthora capsici