DHFR is a relatively small water-soluble protein with a molecular weight of 18.000–25.000 Da. DHFR consists of eight sheets, which form a rigid skeleton: seven sheets run parallel and the other runs antiparallel. All the enzyme isoforms contain at least four α-helices intersecting in the long loops of the sheets. The potential of the dihydrofolate reductase (DHFR) enzyme as a therapeutic target for treating infections has been evidenced. DHFR catalyzes the reduction of dihydrofolate to tetrahydrofolate using NADPH,  an essential cofactor in the biosynthesis of thymidylate monophosphate (dTMP) and it is involved in the synthesis of raw material for cell proliferation, in both prokaryotic and eukaryotic cells.  Inhibition of DHFR leads to a deficiency of dTMP since DHF cannot be recycled, and thus causes inhibition of cell growth.


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