Abstract
The recently discovered non-mevalonate biosynthetic route to isoprenoid precursors is an essential metabolic pathway in plants, apicomplexan parasites, and many species of bacteria. The pathway relies on eight enzymes exploiting different cofactors and metal ions. Structural and mechanistic data now exist for most components of the pathway though there remain some gaps in our knowledge. The individual enzymes represent new, validated targets for broad spectrum antimicrobial drug and herbicide development. Detailed knowledge of the pathway may also be exploited to genetically modify microorganisms and plants to produce compounds of agricultural and medical interest.
Highlights
Isopentenyl pyrophosphate (IPP)2 and dimethylallyl pyrophosphate (DMAPP) are the universal precursors of natural products called isoprenoids
For many years it was assumed that the mevalonate (MVA) pathway was the sole route to IPP and DMAPP
The non-mevalonate pathway starts with condensation of pyruvate and glyceraldehyde 3-phosphate to produce DOXP, catalyzed by 1-deoxy-D-xylulose-5-phosphate synthase (DXS) using thiamine pyrophosphate as cofactor
Summary
Isopentenyl pyrophosphate (IPP)2 and dimethylallyl pyrophosphate (DMAPP) are the universal precursors of natural products called isoprenoids. This pathway is called the non-mevalonate route or alternatively, the 1-deoxy-D-xylulose-5-phosphate (DOXP) or 2C-methyl-D-erythritol-4-phosphate (MEP) pathway. The DOXP pathway consists of eight reactions catalyzed by nine enzymes, seven of which are characterized structurally
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