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Inhibitors of the Herbicidal Target IspD: Allosteric Site Binding

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  • Work at ETH was supported by the Swiss National Science Foundation. IspD=4-Diphosphocytidyl-2C-methyl-D-erythritol synthase, EC 2.7.7.60.

Abstract

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The pick of the pockets: The first inhibitors for IspD, an enzyme from the non-mevalonate pathway of isoprenoid biosynthesis, are described. High-throughput-screening revealed a hit with an IC50 value of 140 nM. Co-crystal structure analyses of the binding mode in the newly formed allosteric pocket (see structure, red ball: water O atom), lead to the synthesis of a set of 17 derivatives which were tested to optimize the herbicidal activity.

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