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 dissociation constant of the ATP analog App(NH)p with myosin is identical to the Km value for ATP hydrolysis, providing insights into myosin-ATP interactions.
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.
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