Uridine 5’-monophosphate (UMP) metabolising enzymes uracil phosphoribosyltransferase and orotidine-5’-phosphate decarboxylase/ump synthase in camels and Trypanosoma evansi

Abstract

In this study, the metabolic pathways and the enzymes involved in uridine 5’-monophosphate (UMP) were investigated in camel and the blood parasite Trypanosoma evansi (T. evansi). The pyrimidine pathway of T. evansi was found to be devoid of uridine kinase and uridine 5-nucleotidase. Since this can affect the de novo synthesis using uracil, salvage enzymes as uracil phosphoribosyltransferase (UPRTase) could be important for the parasite life, given that the similarity rate is not more than 32% between the camel and T. evansi UPRTase. The source of UMP in T. evansi could be from uracil by the action of UPRTase. In addition, the bifunctional orotidine 5’-phosphate decarboxylase (OMPdecase)/UMP synthase shares also in UMP homeostasis. Owing to the diverse sources of UMP in T. evansi, the enzymes involved in UMP metabolism are underscored for drug discovery. However, supported by the lack of uridine kinase, further studies are recommended to estimate the impact of UPRTase inhibition on T. evansi growth.