Abstract
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.
MeSH Terms
Ammonia-Lyases/biosynthesis
Cyclic AMP/metabolism
Enzyme Induction
Enzyme Repression
Histidine Ammonia-Lyase/biosynthesis
Lactates/pharmacology
Pseudomonas/enzymology
Pseudomonas aeruginosa/enzymology
Succinates/pharmacology
Chemicals
Lactates
Succinates
Cyclic AMP
Ammonia-Lyases
Histidine Ammonia-Lyase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Phillips A T
Mulfinger L M
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