An Investigation of the Equilibrium of the Reaction {L-aspartate(aq) + 2-oxoglutarate (aq) = oxaloacetate (aq) + L-glutamate (aq)}

Published

November 1, 1998

Author(s)

N Kishore, Yadu D. Tewari, Robert N. Goldberg

Abstract

Apparent equilibrium constants have been measured for the following biochemical reaction:L-aspartate(aq) + 2-oxoglutarate(aq) = oxaloacetate(aq) + L-glutamate(aq).This reaction, catalyzed by aspartate transaminase, was studied over the ranges 283.15 T/K -1) rG°_m = (4.82 0.21) kJ mo^l-1, the equilibrium constant K = (0.143 0.012), the standard molar enthalpy change δ_rS°_m = -(10 10) J K ^-1, mol^-1 for the following chemical reference reaction at T = 298.15 K and /_m =O:L-aspartate-(aq) + 2-oxoglutarate2-(aq) = oxaloacetate2-(aq) +L-glutamate-(aq).Under near physiological conditions (T = 311.15 K, pH = 7.0, Im = 0.25 mol kg-1) the apparent equilibrium constant K' for the overall biochemical reaction is calculated to have the value 0.147; the standard transformed Gibbs energy change δ_rG°_m = 4.96 kJ mo^l-1 under these conditions.

Citation

Journal of Chemical Thermodynamics

Volume

30

Issue

11

Pub Type

Journals

Keywords

2-oxoglutarate, enthalpy, equilibrium constant, L-aspartate, L-gutamate, oxaloacetate, thermodynamics, transaminase

Citation

Kishore, N. , Tewari, Y. and Goldberg, R. (1998), An Investigation of the Equilibrium of the Reaction {L-aspartate(aq) + 2-oxoglutarate (aq) = oxaloacetate (aq) + L-glutamate (aq)}, Journal of Chemical Thermodynamics (Accessed April 26, 2024)