An official website of the United States government
Here’s how you know
Official websites use .gov
A .gov website belongs to an official government organization in the United States.
Secure .gov websites use HTTPS
A lock (
) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.
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.
Tewari, Y.
, Kishore, N.
, Goldberg, R.
and Luong, T.
(1998),
An Equilibrium and Calorimetric Study of Some Transamination Reactions, Journal of Chemical Thermodynamics
(Accessed June 5, 2023)