title: Cyclic 3',5'-adenosine monophosphate phosphodiesterase of Escherichia coli.
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.
mesh_terms: D000096:Acetone; D000143:Acids; D001426:Bacterial Proteins / Q000494:pharmacology; D003470:Culture Media; D000242:Cyclic AMP; D004789:Enzyme Activation / Q000187:drug effects; D004794:Enzyme Repression; D004926:Escherichia coli / Q000201:enzymology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008722:Methods; D008970:Molecular Weight; D010726:Phosphodiesterase Inhibitors; D010727:Phosphoric Diester Hydrolases / Q000032:analysis / Q000302:isolation & purification*; D013307:Streptomycin; D013997:Time Factors
chemical_list: D000143:Acids; D001426:Bacterial Proteins; D003470:Culture Media; D010726:Phosphodiesterase Inhibitors; D000096:Acetone; D000242:Cyclic AMP; D010727:Phosphoric Diester Hydrolases; D013307:Streptomycin