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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.
Lienhard et al. (Thu,) studied this question.
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