SUMMARY: Experiments have been carried out on the kinetics of induced synthesis of lysine decarboxylase in washed suspensions of The enzyme is produced when glucose and lysine are present simultaneously. Lysine analogues tested as inducers were inactive. In anaerobic synthesis the rate of formation of new enzyme is directly proportional to the degree of saturation of the enzyme by its substrate; in aerobic synthesis a maximal rate is found even when the enzyme is almost totally unsaturated. The pH curve for enzyme synthesis corresponds closely with that for enzyme activity. Adapted cells undergo de-adaptation when incubated with glucose in the absence of lysine; this is due to the effect of cadaverine on the co-enzyme. The bearing of these results on current theories of enzyme induction is discussed.


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