Abstract
Broken cells ofEscherichia coli contain an enzyme system breaking down cyclic 3′,5′-adenosine monophosphate (Ado-3′,5′-P). The enzyme splitting this nucleotide is located in the supernatant fraction at 20,000 ×g. Some characteristics of the enzyme were studied. In contrast with the animal enzyme theEscherichia coli enzyme is not inhibited by caffeine.
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Abbreviations
- Ado-3′,5′:
-
P
- cyclic adenosine 3′,6′:
-
monophosphate.
References
Butcher, R. W., Sutherland, E. W.:Adenosine 3′5′-phosphate in biological materials. I. Purification and properties of cyclic 3′5′-nucleotide phosphodiesterase and use of this enzyme to characterize adenosine 3′5′-phosphate in human urine. J. biol. Chem. 237: 1244, 1962.
Chytil, F., Skřivanová, J.:Reactivation of cortisone induced liver tryptophan pyrrolase by boiled liver cell sap and by cyclic adenosine 3′5′-phosphate. Biochim. biophys. Acta 67: 164, 1963.
Lehman, I. R., Bessman, M. J., Simms, E. S., Kornberg, A.:Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from E. coli. J. biol. Chem. 233: 163, 1958.
Lineweaver, H., Burk, D. J.:The determination of enzyme dissociacion constants. J. Am. chem. Soc. 56: 658, 1934.
Lowry, H. O., Rosebrough, N. J., Farr, A. L., Randall, R.:Protein measurement with the folin phenol reagent. J. biol. Chem. 193:265, 1951.
Makman, R. S., Sutherland, E. W.:Presence of cyclic 3′5′ adenosine phosphate in E. coli. Fed. Proc. 22: 470, 1963.
Mansour, T. E., Mansour, J. M.:Effects of serotonin (5-hydroxytryptamine) and adenosine 3′5′-phosphate on phosphofructokinase from the liver fluke Fasciola hepatica. J. biol. Chem. 237: 629, 1962.
Okabayashi, T., Yoshimoto A., Ide, M.:Occurence of nucleotides in culture fluids of microorganisms. V. Excretion of adenosine cyclic 3′5′-phosphate by Brevibacterium liquefaciens sp.m. J. Bacteriol. 86: 930, 1963a.
Okabayshi, T., Yoshimoto, A., Ide, M.:Excretion of adenosine 3′5′-phosphate in the culture broth of Brevibacterium liquefaciens. Arch. Biochem. Biophys. 100: 158, 1963b.
Rall, T. W., Sutherland, E. W.:Regulatory role of the cyclic 3′5′ adenosine phosphate. Cold Spring Harbor Symposium on Quantitative Biology, 26: 341, 1961.
Roberts, S., Creange, J. E., Fowler, D. D.:Stimulation of steroid C-11 β-hydrozylaseactivity in adrenal homogenates by cyclic 3′5′ adenosine monophosphate. Nature 203: 759, 1964.
Smith, M., Drummond, G. I., Khorana, H. G.:Cyclic phosphates. IV. Ribonucleoside3′5′ cyclic phosphates. A general method of synthesis and some properties. J. Amer. chem. Soc. 83: 698, 1961.
Sutherland, E. W.:Adenyl cyclase —and enzyme with regulatory function. Abstracts of the 6th International congress of Biochemistry, New York, IX, 707, 1964.
Sutherland, E. W., Rall, T. W., Menon, T.:Adenyl cyclase. I. Distribution preparation and properties. J. biol. Chem. 237: 1220, 1962.
Sutherland, E. W., Rall, T. W.:The properties of an adenine nucleotide produced with cellular particles, ATP, Mg2+ and epinephrine or glucagon. J. Amer. chem. Soc. 79: 3608, 1957.
Tryfiates, G. P., Litwack, G.:Appearence of an increment of tyrosine amino transferase activity in a cell-free system. Biochemistry 3: 1483, 1964.
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Braná, H., Chytil, F. Splitting of the cyclic 3′, 5′-adenosine monophosphate in cell-free system ofEscherichia coli . Folia Microbiol 11, 43–46 (1966). https://doi.org/10.1007/BF02877154
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DOI: https://doi.org/10.1007/BF02877154