Cyclic 3′,5′-Adenosine Monophosphate Phosphodiesterase of Escherichia coli-Reference-Cited by-同舟云学术

Cyclic 3′,5′-Adenosine Monophosphate Phosphodiesterase of Escherichia coli

Published:1973-11 Issue:2 Volume:116 Page:857-866
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Nielsen L. D.¹,Monard D.¹,Rickenberg H. V.¹

Affiliation:

1. Division of Research, National Jewish Hospital and Research Center and Department of Biophysics and Genetics, University of Colorado School of Medicine, Denver, Colorado 80206

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.116.2.857-866.1973

Reference20 articles.

1. Cyclic 3,5' adenosine monophosphate-phosphodiesterase and the release of catabolite repression of f-galactosidase by exogenous cyclic 3,5' adenosine monophosphate in Escherichia coli;Aboud M.;Biochem. Biophys. Res. Commun.,1971

2. Pedigrees of some mutant strains of Escherichia coli K-12;Bachmann B. J.;Bacteriol. Rev.,1972

3. Splitting of the cyclic 3', 5'-adenosine monophosphate in a cell-free system of Escherichia coli;Brana H.;Folia Microbiol.,1965

4. Cyclic adenosine 3',5'-monophosphate in Escherichia coli;Buettner M. J.;J. Bacteriol.,1973

5. Oxidative phosphorylation in Escherichia coli K 12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphatase;Butlin J. D.;Biochem. J.,1971

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