Cyclic adenosine 3',5'-monophosphate levels in Pseudomonas putida and Pseudomonas aeruginosa during induction and carbon catabolite repression of histidase synthesis.
Inducibility of histidase (histidine ammonia-lyase, EC 4.3.1.3) in Pseudomonas putida and Pseudomonas aeruginosa was observed to be strongly affected by succinate-provoked catabolite repression, but this did not occur as a consequence of reduced intracellular cyclic adenosine 3',5'-monophosphate levels, and repression could not be alleviated by exogenously added cyclic adenosine 3,'5'-monophosphate. Milder repression of histidase by lactate was also not reversed by the addition of cyclic adenosine 3',5'-monophosphate. These results, along with data showing intracellular cyclic adenosine 3',5'-monophosphate levels remained essentially constant during growth on such diverse carbon sources as histidine, acetamide, glucose, and succinate, indicated that catabolite repression of histidase synthesis by efficient carbon sources was not mediated through variations in internal cyclic adenosine 3,'5'-monophosphate.
D000642:Ammonia-Lyases / Q000096:biosynthesis*; D000242:Cyclic AMP / Q000378:metabolism*; D004790:Enzyme Induction; D004794:Enzyme Repression; D006638:Histidine Ammonia-Lyase / Q000096:biosynthesis*; D007773:Lactates / Q000494:pharmacology; D011549:Pseudomonas / Q000201:enzymology*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D013386:Succinates / Q000494:pharmacology
D007773:Lactates; D013386:Succinates; D000242:Cyclic AMP; D000642:Ammonia-Lyases; D006638:Histidine Ammonia-Lyase