Add time:09/05/2019         Source:sciencedirect.com

A naturally occurring compound, 2'-deoxyadenosine-3'-monophosphate (2'-deoxy-3'-AMP), is a potent inhibitor (Ki about 10 μM) of the adenylate cuclase activity of various rat tissues, toad erythrocytes, and mammalian cells in culture. This inhibition is reversible and appears to be noncompetitive with respect to the substrate, ATP. In addition, in the presence of the inhibitor, adenylate cyclase exhibits negative cooperativity with respect to MgCl2. Cyclase activity stimulated by preincubation with NaF is as sensitive to inhibition by 2'-deoxy-3'-AMP as is control activity. However, preincubation of adenylate cyclase with 5'-guanylylimidodiphosphate (GPPNHP) and isoproterenol reduces its sensitivity to inhibition by the deoxynucleotide. Furthermore, adenylate cyclase exhibits negative cooperativity with respect to inhibition by 2'-deoxy-3'-AMP in the presence but not in the absence of isoproterenol. Finally, the deoxynucleotide inhibitor lowers the observed maximal isoproterenol-stimulated cyclase activity and simultaneously increases the concentration of catecholamine required for half-maximal activation. The possible role of 2'-deoxy-3'-AMP as a regulator of adenylate cyclase and intracellular hormonal responsiveness is discussed.

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