Effect of cyclic adenosine-3',5'-monophosphate on the simultaneous synthesis of beta-galactosidase and tryptophanase in Escherichia coli
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
6243599
DOI
10.1007/bf02876393
Knihovny.cz E-zdroje
- MeSH
- AMP cyklický farmakologie MeSH
- beta-galaktosidasa biosyntéza MeSH
- enzymová indukce účinky léků MeSH
- Escherichia coli účinky léků enzymologie MeSH
- galaktosidasy biosyntéza MeSH
- kinetika MeSH
- lyasy biosyntéza MeSH
- tryptofanasa biosyntéza MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- AMP cyklický MeSH
- beta-galaktosidasa MeSH
- galaktosidasy MeSH
- lyasy MeSH
- tryptofanasa 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
