Effect of cyclic adenosine-3',5'-monophosphate on the simultaneous synthesis of beta-galactosidase and tryptophanase in Escherichia coli
Language English Country United States Media print
Document type Journal Article
PubMed
6243599
DOI
10.1007/bf02876393
Knihovny.cz E-resources
- MeSH
- Cyclic AMP pharmacology MeSH
- beta-Galactosidase biosynthesis MeSH
- Enzyme Induction drug effects MeSH
- Escherichia coli drug effects enzymology MeSH
- Galactosidases biosynthesis MeSH
- Kinetics MeSH
- Lyases biosynthesis MeSH
- Tryptophanase biosynthesis MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Cyclic AMP MeSH
- beta-Galactosidase MeSH
- Galactosidases MeSH
- Lyases MeSH
- Tryptophanase MeSH
When inducing simultaneously beta-galactosidase and tryptophanase in a batch culture either the synthesis of tryptophanase or of both enzymes is decreased due to an insufficient cAMP concentration. The addition of this nucleotide can overcome this decrease. In a continuous culture both enzymes are synthesized at the maximum rate, as the amount of cAMP produced during carbon limitation of growth is probably sufficient for the simultaneous synthesis of both enzymes. In the beta-galactosidase hyperproduction mutant cultivated continuously the level of beta-galactosidase markedly decreases when tryptophanase is simultaneously induced. Also this decrease is caused by cAMP insufficiency and can be overcome by increasing its concentration. cAMP is thus an important regulatory factor of both enzymes and becomes a limiting factor in their simultaneous synthesis; a competition for this regulatory compound apparently occurs and probably also a different mutual affinity of the regulatory complex with the promoter site of the enzyme operons is involved.
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Simultaneous induction of three catabolic enzymes in Escherichia coli
