Abstract: MEP (methylerythritol phosphate) pathway is one of the essential biochemical pathways for the production of the terpenoid precursors isoprenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), and is widespread in plants, bacteria, and pathogens, but absent in mammals. The seven key enzymes of the MEP pathway have been identified as targets for the development of novel pesticides and pharmaceuticals. 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase(IspD) is the third key enzyme of the MEP pathway, which has a low lipophilicity of active sites but unique allosteric sites that have attracted considerable attention from researchers in recent years. Using small molecule inhibitors of IspD to block the MEP pathway and indirectly inhibit the generation of terpenoids can cause the death of pathogens and plants to achieve the purpose of sterilization or weeding. This paper reviews the structure, mechanism, IspD inhibitors and mode of action of the IspD protease. The aim is to provide guidance for the screening of inhibitors targeting IspD and the development of novel pesticides and pharmaceuticals.