A 5'-Adenosine Monophosphate-Dependent Adenylate Cyclase and an Adenosine 3':5'-Cyclic Monophosphate-Dependent Adenosine Triphosphate Pyrophosphohydrolase in Dictyostelium discoideum.
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.
Department of Biology, Brandeis University, Waltham, Massachusetts 02154.
E F
EF
Rossomando
M
M
Sussman