Insights into structural features of Plasmodium falciparum 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase enzyme

Malaria remains one of the most serious infectious diseases in the world. Though there are four species of Plasmodium genus, but the most responsible and virulent among them is Plasmodium falciparum. The unique biochemical processes that exist in Plasmodium falciparum provide a useful way to develop novel inhibitors. One such biochemical pathway is methyl erythritol phosphate (MEP) pathway, required to synthesize isoprenoids. In the present study a detailed computational analysis has been performed for 4-hydroxy-3methylbut-2-en-1-yl diphosphate synthase, a key enzyme in MEP pathway. The structural properties, secondary structure and evolutionary conservation of the enzyme were studied. The homology model of the enzyme was also developed.