The dissociation constant of adenylyl imidodiphosphate with myosin was 0.400 ± 0.040 PM, identical to the previously reported Km value for ATP hydrolysis.
The binding of adenylyl imidodiphosphate (App(NH)p), an analog of ATP with an imido group (-NH-) in place of the terminal oxygen bridge, to myosin and heavy meromyosin was studied.Binding studies were performed at 23-25" in 0.020 M Tris-HCl, 1.00 mM MgS04, and 0.100 M NaCl at pH 7.4.The dissociation constant of App(NH)p with myosin, 0.400 + 0.040 PM, is identical with the previously reported K,,, value for ATP hydrolysis, 0.41 PM (SCHLISELFELD, L., AND
Louis H. Schliselfeld (Thu,) reported a other. Adenylyl imidodiphosphate (App(NH)p) was evaluated on Dissociation constant of App(NH)p with myosin. The dissociation constant of adenylyl imidodiphosphate with myosin was 0.400 ± 0.040 PM, identical to the previously reported Km value for ATP hydrolysis.