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Adenosine 3′,5′-cyclic monophosphate (cyAMP) and the cyAMP-binding protein are necessary for efficient induction ofd -serine deaminase (Dsdase) synthesis indsdC + dsdO + anddsdC dsdO + strains ofEscherichia coli K-12, and for constitutive synthesis indsdC dsdO + strains. Neither is required indsdO strains, confirming previous indications that indsdO mutants Dsdase synthesis is not subject to catabolite repression control. Since efficient Dsdase synthesis indsdC + anddsdC strains that aredsdO + requires the cyAMP-binding protein, which acts at the level of transcription in other systems, it is concluded that catabolite repression acts at the level of transcription of the Dsdase structural gene. Since catabolite repression is reversed by the inducer,d -serine indsdC dsdO + strains, it is concluded that induction also acts at the level of transcription in this system. ThedsdC strains were found to be much more sensitive to induction byd -serine than aredsdC + strains under conditions of catabolite repression, whether the repression was caused by glucose or by loss of ability to form cyAMP or cyAMP-binding protein. This suggests that ad -serine-dsdC complex may be able to replace partially the cyAMP:cyAMP-binding protein action in initiation of Dsdase messenger ribonucleic acid synthesis—a positive control effect.

Role of Adenosine 3′,5′-Cyclic Monophosphate and Its Specific Binding Protein in the Regulation of d -Serine Deaminase Synthesis