1Department of Biomedical Sciences, College of Veterinary Medicine, King Faisal University, Alahsa, 31982, Saudi Arabia
2Department of Pharmacology, Faculty of Veterinary Medicine, Kafrelsheikh University, Kafrelsheikh, 35255, Egypt
*SEND REPRINT REQUEST TO MAHMOUD KANDEEL email: mkandeel@kfu.edu.sa
Bifunctional protein can be used as a drug target as it proves a classical difference between the host and parasite structures that can be used as a drug target. In this study, the metabolic pathways of deoxyuridine 5-monophosphate (dUMP) were compared in camel and the blood parasite Trypanosoma evansi. T. evansi shares similar profile with camel pathways but with predicted inability to degrade dUMP to uridine and devoid of dCTP deamination to yield dUMP. In the enzyme set of dUMP metabolism, thymidylate synthase was raised as a bifunctional enzyme in T. evansi with dihydrofolate reductase-thymidylate synthase (DHFR-TS) domains content, compared to a single TS domain in camels enzyme. Specific targeting of DHFR-TS in T. evansi is expected to yield specific anti-trypanosomal drugs.
Camel, DHFR-TS, DUTP, Thymidylate synthase, Trypanosoma evansi
