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An Equilibrium and Calorimetric Study of Some Transamination Reactions

Published

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

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 April 19, 2024)
Created June 1, 1998, Updated February 17, 2017