[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.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D000242:Cyclic AMP / Q000031:analogs & derivatives*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008968:Molecular Conformation; D011485:Protein Binding; D051381:Rats; D013329:Structure-Activity Relationship
D000242:Cyclic AMP; D015105:3',5'-Cyclic-AMP Phosphodiesterases
Vzaimodeĭstvie fosfodiesterazy tsiklicheskogo adenozin-3':5'-monofosfata so strukturnymi analogami substrata.