Key result
The dissociation constant of adenylyl imidodiphosphate with myosin was 0.400 ± 0.040 PM, identical to the previously reported Km value for ATP hydrolysis.
Population
Myosin and heavy meromyosin
Design
Preclinical
Authors
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Should not alter clinical myosin-targeted therapies; leaves open whether App(NH)p binding extends to human cardiac function in vivo.
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.
Louis H. Schliselfeld (1974) studied this question. 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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