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  • Title: Muscle adenylate kinase catalyzes adenosine 5'-tetraphosphate synthesis from ATP and ADP.
    Author: Kupriyanov VV, Ferretti JA, Balaban RS.
    Journal: Biochim Biophys Acta; 1986 Jan 17; 869(1):107-11. PubMed ID: 3002476.
    Abstract:
    Muscle adenylate kinases from rabbit and porcine sources were found by NMR to catalyze the formation of adenosine tetraphosphate (5'AdoP4) from adenosine triphosphate (ATP) and adenosine diphosphate (ADP). The reaction was completely reversible, with an equilibrium constant of approx. 0.1 at 30 degrees C. The synthesis of 5'AdoP4 from ATP and ADP occurred very slowly, taking over 12 h to reach equilibrium under the conditions used in this study. The sources of micromolar concentrations of 5'AdoP4 found in biological tissues is unknown: potentially, the slow adenylate-kinase-catalyzed breakdown and synthesis of 5'AdoP4 may serve as an important regulator of the steady-state concentration of 5'AdoP4 in muscle tissue.
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