Cyclic 3′,5′-Adenosine Monophosphate Phosphodiesterase of Escherichia coli
- 1 November 1973
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 116 (2), 857-866
- https://doi.org/10.1128/jb.116.2.857-866.1973
Abstract
The cyclic 3′,5′-adenosine monophosphate (c-AMP) phosphodiesterase from Escherichia coli has been partially purified. The enzyme has an apparent molecular weight of 30,000, a Michaelis constant of 0.5 mM c-AMP, and a pH optimum of 7. The partially purified enzyme requires for activity the presence of a reducing compound and of either iron or a protein which seemingly acts as iron carrier.Keywords
This publication has 14 references indexed in Scilit:
- Cyclic Adenosine 3′,5′-Monophosphate in Escherichia coliJournal of Bacteriology, 1973
- Pedigrees of some mutant strains of Escherichia coli K-12Microbiology and Molecular Biology Reviews, 1972
- Oxidative phosphorylation in Escherichia coli K 12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphataseBiochemical Journal, 1971
- CYCLIC AMPAnnual Review of Biochemistry, 1971
- Cyclic 3′;5′ adenosine monophosphate-phosphodiesterase and the release of catabolite repression of β-galactosidase by exogenous cyclic 3′;5′ adenosine monophosphate in escherichia coliBiochemical and Biophysical Research Communications, 1971
- Cyclic 3′,5′-nucleotide phosphodiesteraseBiochemical and Biophysical Research Communications, 1970
- The enzymic degradation of 3′, 5′ cyclic AMP in strains ofBiochemical and Biophysical Research Communications, 1969
- Catabolite repression in Escherichiacoli: The role of glucose 6-phosphateBiochemical and Biophysical Research Communications, 1967
- Splitting of the cyclic 3′, 5′-adenosine monophosphate in cell-free system ofEscherichia coliFolia Microbiologica, 1966
- Genetic control of catabolite repression of the lac operon in EscherichiacoliBiochemical and Biophysical Research Communications, 1965