Effects of 8-substituted analogs of cyclic adenosine 3',5'-monophosphate on in vivo and in vitro syntheses of beta-galactosidase in Escherichia coli.
AUTOR(ES)
Ito, T
RESUMO
Several 8-substituted alkylthio and alkylamino cyclic adenosine 3',5'-monophosphate (cAMP) derivatives were tested for their ability to stimulate beta-galactosidase synthesis in Estherichia coli in vivo and in vitro and to inhibit the cAMP phosphodiesterase activity of E. coli. Stimulation of beta-galactosidease synthesis in vivo by cAMP derivatives decreased with increasing length of the unbranched carbon chain of the substituent. On the other hand, the stimulation in vitro was increased as the carbon chain elongated. The 8-decylthio- and 8-dodecylthio-cAMP compounds stimulated beta-galactosidase synthesis almost eight-fold compared with cAMP, whereas 8-undecyl-, 8-dodectyl-, and 8-tridecylamino-cAMP stimulated beta-galactosidase synthesis about threefold. However, in in vitro experiments with a phosphodiesterase-deficient strain of E. coli, the Crooks strain, the stimulatory effects of the derivatives disappeared, except for 8-dodecylthio cAMP which stimulated beta-galactosidase about 1.4- to 1.6-fold. All derivatives were quite resistant to hydrolysis by phosphodiesterase. Most derivatives competitively inhibited the hydrolysis of cAMP by phosphodiesterase.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=218089Documentos Relacionados
- Cyclic Adenosine 3′,5′-Monophosphate in Escherichia coli
- Cyclic adenosine 3',5'-monophosphate regulation of membrane energetics in Escherichia coli.
- Effect of glucose and its analogues on the accumulation and release of cyclic adenosine 3',5'-monophosphate in a membrane fraction of Escherichia coli: relation to beta-galactosidase synthesis.
- Suppression of defects in cyclic adenosine 3',5'-monophosphate metabolism in Escherichia coli.
- Metabolism of cyclic adenosine 3',5'-monophosphate and induction of tryptophanase in Escherichia coli.