1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR)

1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), also known as IspC, is an enzyme that catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to form 2-C-methyl-D-erythritol 4-phosphate (MEP). This is a crucial step in the MEP pathway for isoprenoid biosynthesis, found in many bacteria, algae, plants, and some protozoa like *Plasmodium falciparum*. DXR is essential for producing IPP and DMAPP, building blocks for terpenoids. It's a homodimer with three domains: a dinucleotide-binding domain, a connective domain for dimerization/active site formation, and a four-helix bundle domain. DXR is inhibited by fosmidomycin, making it an attractive target for antimicrobial drug development, particularly against malaria and bacterial infections, because humans use the mevalonate pathway instead.

Other names

IspCDXR reductoisomerase1-Deoxyxylulose-5-phosphate reductoisomerase

Competitive inhibitor of DXP binding