[Interaction between cyclic adenosine-3':5'-monophosphate phosphodiesterase and structural analogs of the substrate].

The interaction between synthetic structural analogs of cyclic adenosine-3':5'-monophosphate (3':5'-AMP) and rat liver 3':5'-AMP phosphodiesterase was studied. Various groups, including those capable of covalent binding to the protein, were injected into certain sites of the 3':5'-AMP molecule. All the compounds tested exerted an inhibiting effect; in seven cases this effect was irreversible. Some peculiarities of 3':5'-AMP binding in the enzyme active center are discussed.