Abstract
IspE kinase inhibitors. The first inhibitors for the kinase IspE, an enzyme of the non-mevalonate pathway, are presented. The nonphosphate based inhibitors avoid binding to the ATP site but instead occupy the substrate site and a small, newly detected hydrophobic subpocket at the active site of IspE. With appropriate filling of this pocket, competitive inhibition constants Kic in the upper nanomolar range are measured.
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