Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. It can only hydrolyze L,L-N-succinyl-diaminopimelic acid (L,L-SDAP) and is inactive toward D,L-, L,D-, and D,D-SDAP. H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate Binds 2 Zn(2+) ion per subunit. Competitively inhibited by L,L-DAP, D,L-DAP, 2-carboxyethylphosphonic acid (CEPA) and 5-mercaptopentanoic acid (MSPA). Succinate is a poor inhibitor. Optimum pH is 7.0 in the presence of Zn(2+). The maximal velocities are independent of pH in the alkaline region but decrease below pH 7.0. Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3. Homodimer. Belongs to the peptidase M20A family. DapE subfamily.