Adenylate cyclase activity was detected and characterized in cell-free preparations of different strains of Escherichia coli; it was localized not only in the membrane fraction but also in the cytoplasm, the localization differing from strain to strain. The adenylate cyclase activity is highly dependent on the method used for disintegration of cells. The best results were obtained when using vortexing of the cell suspension with ballotini beads. The pH optimum of adenylate cyclase in cell-free preparations was found to be 9.0--9.5. The enzyme has an absolute requirement for Mg2+ and is inhibited by sodium fluoride and inorganic diphosphate. Release of adenylate cyclase from the membrane leads to an immediate loss of the activity; it was found that adenylate cyclase is quite labile and hence it could not yet been purified. The method used to determine adenylate cyclase activity and cyclic AMP is described.

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Biochim Biophys Acta. 1951 May;7(1):153-74 PubMed

Biochem Biophys Res Commun. 1975 Jan 2;64(3):845-50 PubMed

Biochim Biophys Acta. 1974 Apr 25;341(2):388-95 PubMed

Arch Biochem Biophys. 1970 Nov;141(1):236-40 PubMed

Proc Natl Acad Sci U S A. 1969 May;63(1):86-92 PubMed

J Pharmacol Exp Ther. 1968 Oct;163(2):379-85 PubMed

Folia Microbiol (Praha). 1969;14(3):185-9 PubMed

Biochem Biophys Res Commun. 1965 Nov 22;21(4):361-5 PubMed

Biochem Biophys Res Commun. 1969 Jul 7;36(1):42-6 PubMed

Biochim Biophys Acta. 1967 Nov 21;149(1):1-11 PubMed

J Biol Chem. 1969 Dec 10;244(23):6395-402 PubMed

Bacteriol Rev. 1976 Sep;40(3):527-51 PubMed

J Bacteriol. 1973 Nov;116(2):857-66 PubMed

Proc Natl Acad Sci U S A. 1970 Sep;67(1):305-12 PubMed

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The control of adenylate cyclase activity in Escherichia coli