Abstract
The effect of L-leucine on L-lysine production was investigated in Brevibacterium lactofermentum.L-Lysine production was inhibited by L-leucine specifically, and this inhibition was recovered completely by L-valine. The present study indicated that the inhibition of L-lysine production by the addition of excess L-leucine was accompanied with the repression of dihydrodipicolinate (DDP) synthetase. DDP synthetase was the first specific enzyme in lysine biosynthesis.On the other hand, α-isopropylmalate (IPM) synthetase, which was the key enzyme and the first specific enzyme in leucine biosynthesis was inhibited by L-leucine, while L-lysine caused the complete reversion from its inhibition.From the above results, the possible physiological meanings of this coregulation mechanism of lysine and branched-chain amino acids biosynthesis in B. lactofermentum was discussed.
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