Publication | Open Access
P1,P5-Di(adenosine-5′)pentaphosphate, a Potent Multisubstrate Inhibitor of Adenylate Kinase
521
Citations
9
References
1973
Year
Muscle FunctionCellular PhysiologyAdenylate KinaseMolecular PharmacologyMuscle PhysiologySkeletal MuscleCell SignalingAssociation ConstantCell PhysiologyHealth SciencesMolecular PhysiologyBiochemistryG Protein-coupled ReceptorIon ChannelsPharmacologyProtein PhosphorylationPolyphosphate BridgeSignal TransductionPhysiologyX 108Cellular BiochemistryMedicine
Abstract Rabbit muscle adenylate kinase is potently inhibited by P1,P5-di(adenosine-5')pentaphosphate (Ap5A) but not by the homologs of this compound with fewer phosphoryl groups in the polyphosphate bridge and not by adenosine 5'-pentaphosphate. The inhibition by Ap5A is competitive with respect to both of the substrates, AMP and ATP. The association constant for the binding of Ap5A to adenylate kinase is about 4 x 108 m-1 at 24° and pH 8.0.
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