Characterization and cAMP inhibition of a lysyl-(N-epsilon-5'-phospho) adenosyl phosphoamidase in Dictyostelium discoideum.
A lysyl-(N-epsilon-5'-phospho) adenosyl phosphoamidase activity has been identified in Dictyostelium discoideum. Conjugates, formed by coupling AMP via a phosphoamide bond to the epsilon amino group of lysine in avidin and tuftsin, served as substrate. Lysyl-N-epsilon-5'-phosphoadenosine and adenosine phosphoramidate (AMPNH) were substrates as well. The phosphoamidase liberated AMP from all four compounds but did not degrade cAMP. Approximately 90% of the phosphoamidase activity was inhibited competitively by 100 microM cAMP with an apparent Ki of 35 microM for all substrates.
D002851:Chromatography, High Pressure Liquid; D000242:Cyclic AMP / Q000494:pharmacology*; D004023:Dictyostelium / Q000201:enzymology*; D006867:Hydrolases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology; D013379:Substrate Specificity
D008670:Metals; D000242:Cyclic AMP; D006867:Hydrolases; C049250:lysyl-(N-epsilon-5'-phospho) adenosyl phosphoamidase