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. 1973 Apr;70(4):1254–1257. doi: 10.1073/pnas.70.4.1254

A 5′-Adenosine Monophosphate-Dependent Adenylate Cyclase and an Adenosine 3′:5′-Cyclic Monophosphate-Dependent Adenosine Triphosphate Pyrophosphohydrolase in Dictyostelium discoideum

Edward F Rossomando 1,*, Maurice Sussman 1
PMCID: PMC433470  PMID: 16592080

Abstract

Cell aggregation in Dictyostelium discoideum appears to involve the production and detection of 3′:5′-cyclic AMP. Two pertinent catalytic activities have been studied in concentrates from D. discoideum purified 50- to 100-fold. They are (i) adenylate cyclase and (ii) ATP pyrophosphohydrolase. ATP pyrophosphohydrolase activity converts ATP to 5′-AMP and pyrophosphate. The presence of 5′-AMP is an absolute requirement for adenylate cyclase activity. The presence of 3′:5′-cyclic AMP is an absolute requirement for ATP pyrophosphohydrolase activity. Both activations, particularly that of ATP pyrophosphohydrolase, show narrow ranges of specificity and display significant cooperativities.

Keywords: chemotaxis, enzyme regulation, phosphodiesterase, 5′-nucleotidase, Polysphondylium violaceum

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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