Abstract
A CRITICAL ratio of magnesium and the adenosine phosphates has been observed in several enzymically catalysed reactions. Hers1 demonstrated that maximal activity in the hexokinase and fructokinase reactions occurred when the magnesium/adenosine triphosphate ratio was one. The rate of formation of adenosine diphosphate from adenosine monophosphate and adenosine triphosphate, catalysed by myokinase, was maximal when the magnesium /adenosine triphosphate ratio was one; in the reverse reaction, maximal activity was observed when the ratio was one half2. A definite stoichiometry between adenosine triphosphate and manganese also has been found, for Lowenstein3 observed that maximal activity in a non-enzymic transphosphorylation occurred when the manganese/adenosine triphosphate ratio was approximately 1.7.
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References
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MUDD, J. Interaction of Magnesium and Adenosine Diphosphate in Photosynthetic Phosphorylation. Nature 183, 900–901 (1959). https://doi.org/10.1038/183900a0
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DOI: https://doi.org/10.1038/183900a0
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