Abstract: N-Succinyl-L,L-diaminopimelic acid desuccinylase (DapE) encoded by dapE is a metal-dependent hydrolase and a key enzyme in the bacterial meso-diaminopimelic(m-DAP)/lysine biosynthetic pathway. DapE catalyzes hydrolysis of N-succinyl-L,L-diaminopimelic acid to form L,L-diaminopimelic acid and succinic acid, which are essential for the further synthesis of peptidoglycan and lysine. Knocking out the dapE will block lysine biosynthesis in bacteria and prevent most bacterial cell walls/protein from synthesizing the required m-DAP/lysine, thus affecting normal bacterial growth and reproduction. As there are no similar biosynthetic pathways in mammals, inhibiting DapE could selectively target bacteria while leaving humans and other mammals unaffected. In this review, we summarize the importance, three-dimensional structure, active site, catalytic mechanism and inhibitors targeting DapE in bacterial m-DAP/lysine biosynthetic pathway with a view to providing guidance for the discovery of lead compounds targeting DapE and and the design ofactive molecules for pesticides against plant bacterial diseases.