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Regulation of dihydrodipicolinate synthase and diaminopimelate decarboxylase activity in Bacillus stearothermophilus.

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.