Open AccessA 5′-Adenosine Monophosphate-Dependent Adenylate Cyclase and an Adenosine 3′:5′-Cyclic Monophosphate-Dependent Adenosine Triphosphate Pyrophosphohydrolase in Dictyostelium discoideum
Author(s) -
Edward F. Rossomando,
Maurice Sussman
Publication year - 1973
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.70.4.1254
Subject(s) - dictyostelium discoideum , adenylate kinase , adenosine , cyclase , adcy3 , adcy6 , adenosine monophosphate , adenosine triphosphate , biochemistry , chemistry , microbiology and biotechnology , biology , enzyme , adcy9 , adenylyl cyclase , gene
Cell aggregation inDictyostelium discoideum appears to involve the production and detection of 3′:5′-cyclic AMP. Two pertinent catalytic activities have been studied in concentrates fromD. 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.