
Magnesium, Potassium, and the Adenylate Kinase Equilibrium
Author(s) -
Blair J. McD.
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb00940.x
Subject(s) - adenylate kinase , equilibrium constant , chemistry , magnesium , nucleotide , potassium , phosphofructokinase , adenine nucleotide , pyrophosphate , enzyme , thermodynamics , biochemistry , inorganic chemistry , glycolysis , physics , organic chemistry , gene
1 The influence of magnesium and potassium on the equilibrium catalysed by adenylate kinase has been studied. An equation has been derived which describes the effect of these ions on the equilibrium; values for the metal‐nucleotide stability constants, and for the “true” equilibrium constant, [AMP 2− ] · [ATP 4− ]/([ADP 3− ]) 2 , have been calculated, which give the best fit of this equation to the experimental data. 2 Using these constants, the concentrations of all significant species in an adenine nucleotide pool equilibrated by adenylate kinase can be calculated, for any specified total concentrations of magnesium, potassium, and adenine nucleotide pool, at any pH and any pyrophosphate bond content of the adenine nucleotide pool. Magnesium emerges as a significant feedback signal from an adenine nucleotide pool considered as an isolated system. 3 The possible significance of this data with respect to the control of metabolic flux in general and of phosphofructokinase in particular is discussed.