SUMMARY: Induction of ethanolamine ammonia-lyase formation in required both ethanolamine and vitamin B, and was gratuitous during growth on glycerol. Ethanolamine analogues inhibited enzyme activity and inhibited growth with ethanolamine as the nitrogen source, but did not act as inducers. Enzyme formation was more rapid when ethanolamine was added to cultures containing vitamin B rather than the reverse. Enzyme formation was subject to catabolite repression, glucose and acetate being particularly effective. Chloramphenicol, I-aminopropan-2-ol and 1,3-diaminopropan-2-ol prevented enzyme induction. Ethanolamine ammonia-lyase, resolved from its cobamide coenzyme, was purified 35-fold. The apoenzyme was stable for several days in the presence of ethanolamine, dithio-threitol, glycerol and K ions.

Enzyme formation therefore requires both substrate and cobamide coenzyme to be present simultaneously as inducers.


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