A Thermodynamic Study of the Hydrolysis of L-Glutamine to (L-Glutamate + Ammonia) and of L-Asparagine to (L-Aspartate + Ammonia)

Published

September 1, 2000

Author(s)

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

Abstract

Calorimetric enthalpies of reaction have been measured for the following enzyme-catalyzed reactions:L-glutamine(aq) + H₂O(l) = L-glutamate(aq) + ammonia(aq),L-asparagine(aq) + H₂O(l) = L-aspartate(aq) + ammonia(aq).An equilibrium model that accounted for the multiplicity of ionic forms of the reactants and products was used to calculate standard molar enthalpies for reference reactions involving specific species. Values of equilibrium constants for the reference reactions were obtained using results from the literature in thermochemical cycle calculations. The thermodynamic results are discussed in relation to the structural changes involved in these reactions.

Citation

Journal of Chemical Thermodynamics

Volume

32

Issue

No. 9

Pub Type

Journals

Keywords

ammonia, asparaginase, enthalpy, equilibrium constants, glutaminase, L-asparagine, L-aspartate, L-glutamate, L-glutamine

Citation

Kishore, N. , Tewari, Y. and Goldberg, R. (2000), A Thermodynamic Study of the Hydrolysis of L-Glutamine to (L-Glutamate + Ammonia) and of L-Asparagine to (L-Aspartate + Ammonia), Journal of Chemical Thermodynamics (Accessed April 25, 2024)