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Science 3 March 1972:
Vol. 175. no. 4025, pp. 1016 - 1018
DOI: 10.1126/science.175.4025.1016
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Articles

Cyclic Nucleotide Phosphodiesterase in Dictyostelium discoideum: Interconversion of Two Enzyme Forms

Bruce M. Chassy 1

1 Environmental Mechanisms Section, National Institute of Dental Research, Bethesda, Maryland 20014

An extracellular cyclic nucleotide phosphodiesterase was isolated from either growing cultures or aggregating amoebas of Dictyostelium discoideum. The enzyme is released in a form with a low Michaelis constant (15 micromolar) and spontaneously undergoes a slow conversion to a less active form with a high Michaelis constant (2 mnillimolar). Inactivation was prevented or reversed by use of Cleland's reagent, dithiothreitol. The two enzyme forms may be part of a mechanism for control of concentration of cyclic adenosine monophosphate.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A Cysteine-Rich Extracellular Protein Containing a PA14 Domain Mediates Quorum Sensing in Dictyostelium discoideum.
A. Kolbinger, T. Gao, D. Brock, R. Ammann, A. Kisters, J. Kellermann, D. Hatton, R. H. Gomer, and B. Wetterauer (2005)
Eukaryot. Cell 4, 991-998
   Abstract »    Full Text »    PDF »
Phosphodiesterase in Dictyostelium discoideum and the Chemotactic Response to Cyclic Adenosine Monophosphate.
R. G. Pannbacker and L. J. Bravard (1972)
Science 175, 1014-1015
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)