Equilibrium constants of the reactions of acetyl coenzyme A synthetase and the hydrolysis of adenosine triphosphate to adenosine monophosphate and inorganic pyrophosphate.
نویسندگان
چکیده
The observed standard free energy change (AGtbs) for the ATP-pyrophosphorylase reaction (EC 3.6.1.8) has been calculated for near physjological conditions of temperature, ionic strength, and free magnesium concentration. The observed equilibrium constant (Kobs) for the acetyl-CoA synthetase reaction (EC 6.2.1.1) has been determined at both 25 and 38”, pH 7.0, ionic strength 0.25, and varying free [Mg’+]. The Kobs o f this reaction reflects the difference between the AGtbS for the hydrolysis of acetyl-CoA and the AGO ,,I,* for the hydrolysis of ATP to AMP and inorganic PPi. Using c and square brackets to indicate total concentrations of all the ionic species present:
منابع مشابه
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 249 10 شماره
صفحات -
تاریخ انتشار 1974