Herbicide-resistant weeds are becoming a widespread problem, resulting in decreased crop yield and quality. Therefore, there is an urgent need to discover novel herbicides and an equally urgent need to identify new targets with no pre-existing resistance mechanisms. One such target is the diaminopimelate (DAP) pathway involved in lysine biosynthesis, found exclusively in plants and bacteria. Dihydrodipicolinate synthase (DHDPS) catalyses the rate limiting step in the DAP pathway. Recently, we have identified inhibitors of bacterial DHDPS with promising antimicrobial activity that are non-toxic to human cells. Given that the active site is highly conserved amongst DHDPS orthologues, it is hypothesised that these inhibitors have a similar effect on noxious weeds and could represent novel classes of broad spectrum herbicides. In this study, the model plant, Arabidopsis thaliana (At), was employed to assess the effect of our inhibitors against plant DHDPS. Firstly, AtDHDPS was overexpressed in E. coli (BL21) cells with GroEL/ES chaperonins and the recombinant product was purified using nickel affinity and size exclusion chromatography. Circular dichroism spectroscopy and analytical ultracentrifugation studies demonstrate that the recombinant AtDHDPS is folded and exists as a tetramer in solution. Enzyme kinetic studies demonstrate that these inhibitors have micromolar potency against AtDHDPS, which are the most potent plant DHDPS inhibitors discovered to date. Co‑crystallisation of AtDHDPS + inhibitors will follow to guide the design of more potent analogues. Future studies will also examine the propensity of these compounds to inhibit DHDPS in planta.