The feedback inhibition of the enzymes dihydrodipicolinate (DHDPS) and diaminopimelate decarboxylase (DAPD) in the wild strain Zu 183 of Bacillus stearothermophilus and in its S-(2-aminoethyl)-cysteine resistant L-lysine overproducing strain AEC 12 was studied. The optimum temperature and pH of both enzymes were also evaluated. No inhibition of DHDPS by L-lysine, L-threonine, L-methionine and L-isoleucine was observed either in the wild strain or in the AEC 12 mutant. DAPD was completely inhibited by L-lysine and only partially by L-threonine and L-methionine in Zu 183 and AEC 12 strains, but the concentration required was found to be much higher in the AEC 12 strain. The regulation mechanism of L-lysine biosynthesis in Bacillus stearothermophilus Zu 183 was also discussed.