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Thermodynamics of Reactions Catalyzed by Branched-Chain-Amino-Acid Transaminase
Published
Author(s)
Yadu D. Tewari, Robert N. Goldberg, J D. Rozzell
Abstract
Apparent equilibrium constants and calorimetric enthalpies of reaction have been measured for reactions catalyzed by branched-chain-amino-acid transaminase. The following biochemical reactions have been studied at the temperature 298.15 K and in the pH range (7.15 to 7.24): L-valine(aq) + 2-oxoglutarate(aq) = 2-oxoisovalerate(aq) + L-glutamate(aq); L-leucine(aq) + 2-oxoglutarate(aq) = 2-oxoisocaproate(aq) + L-glutamate(aq); and L-tert-leucine(aq) + 2-oxoglutarate(aq) = 3,3-dimethyl-2-oxobutanoate(aq) + L-glutamate(aq). The results have been used to calculate equilibrium constants and standard molar enthalpy,δrHo/m entropy, δrSo/m and Gibbs free energy δrGo/m changes for reference reactions involving specific species. Apparent equilibrium constants and standard transformed Gibbs energy changes for these reactions under physiological conditions have also been calculated. The use of these results for optimization of product yields of the branched-chain amino acids is discussed.
Tewari, Y.
, Goldberg, R.
and Rozzell, J.
(2000),
Thermodynamics of Reactions Catalyzed by Branched-Chain-Amino-Acid Transaminase, Journal of Chemical Thermodynamics
(Accessed September 22, 2023)