Abstract
The unique methylerythritol phosphate (MEP) pathway for isoprenoid biosynthesis is essential in most human pathogens, including Mycobacterium tuberculosis and the malaria parasite Plasmodium falciparum. The first enzyme in this pathway, 1‐deoxy‐D‐xylulose 5‐phosphate (DXP) synthase, catalyzes the thiamin diphosphate (ThDP)‐dependent formation of DXP from D‐glyceraldehyde 3‐phosphate (GAP) and pyruvate. This enzyme is mechanistically and structurally distinct from other ThDP‐dependent enzymes and is a potential drug target for the development of new anti‐infective agents. Toward our long‐term goal to target non‐mammalian isoprenoid biosynthesis, we have conducted mechanistic studies of DXP synthase. Here, we present the results of detailed kinetic analysis and substrate binding studies. Our work suggests a novel, random sequential mechanism of catalysis for DXP synthase.
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