An Equilibrium and Calorimetric Study of Some Transamination Reactions

Published

June 1, 1998

Author(s)

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

Abstract

Apparent equilibrium constants and calorimetric enthalpies of reaction have been measured for the following enzyme-catalyzed biochemical reactions at the temperature 298.15 k:l-alanine(aq) + 2-oxoglutarate(aq) = pyruvate(aq) + L-glutamate(aq); L-tyrosine(aq) + 2-oxoglutarate(aq) = 4hydroxyphenylpyruvate(aq) + L-glutamate(aq); and L-phenylalanine(aq) + 2-oxoglutarate(aq) = phenylpyruvate(aq) + L-glutamate(aq).The results are used to calculate equilibrium constants and standard molar enthalpy, entropy, and Gibbs energy 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 results are discussed in terms of the changes in chemical bonding characteristic of transamination reactions.

Citation

Journal of Chemical Thermodynamics

Volume

30

Issue

6

Pub Type

Journals

Keywords

2-oxoglutrate, 4-hydroxyphenylpyruvate, aminotransferase, enthalpy, equilibrium constant, L-alanine, L-glutamate, L-phenylalanine, phenylpyruvate

Citation

Tewari, Y. , Kishore, N. , Goldberg, R. and Luong, T. (1998), An Equilibrium and Calorimetric Study of Some Transamination Reactions, Journal of Chemical Thermodynamics (Accessed January 22, 2026)