The equilibrium constants of the glutamate dehydrogenase systems

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Abstract
Equilibrium constants for the oxidation of glutamate by NAD+ and NADP+, catalyzed by [ox liver] glutamate dehydrogenase were measured in phosphate buffers of different ionic strengths and at several temperatures. The equilibrium constants for both systems vary markedly with ionic strength. Thermodynamic values for the 2 systems obtained by extrapolation to zero ionic strength differ significantly from one another. The standard free-energy change for NADP+ reduction was calculated from that for NAD+ reduction. The heat of reaction was estimated and is the same with both coenzymes. The thermodynamic data are discussed in relation to earlier data.