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February 1, 1973Journal of Biological Chemistry522 citationsOpen Access

P1,P5-Di(adenosine-5′)pentaphosphate, a Potent Multisubstrate Inhibitor of Adenylate Kinase

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GLGustav E. LienhardISIsaac I. Secemski

Key Points

  • The aim is to assess the inhibitory effects of P1,P5-di(adenosine-5')pentaphosphate on adenylate kinase.
  • Determined the inhibition potency of Ap5A on rabbit muscle adenylate kinase.
  • Examined the competitiveness of Ap5A against substrates AMP and ATP.
  • Calculated the association constant for Ap5A binding at 24° and pH 8.0.
  • Ap5A strongly inhibits adenylate kinase, with a competitive inhibition profile regarding AMP and ATP.
  • The association constant for Ap5A binding to adenylate kinase is about 4 x 10^8 m-1.

Abstract

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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Cite This Study

Lienhard et al. (1973) studied this question.

synapsesocial.com/papers/6a0227a3f58f6e6cfdd8dbb2https://doi.org/10.1016/s0021-9258(19)44380-9
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