Thermodynamics and Kinetics of the Glyoxylate Cycle

Robert A. Alberty*
Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139
Biochemistry, 2006, 45 (51), pp 15838–15843
DOI: 10.1021/bi061829e
Publication Date (Web): December 5, 2006
Copyright © 2006 American Chemical Society

 This research was supported by NIH grant 5-RO1-GM48358-10.

,
*

 Corresponding Author. E-mail:  alberty@mit.edu. Telephone:  617-253-2456. Fax:  617-253-7030.

Abstract

Abstract Image

Because the standard Gibbs energies of formation of all the species of reactants in the glyoxylate cycle are known at 298.15 K, it is possible to calculate the apparent equilibrium constants of the five reactions in the cycle in the pH range 5−9 and ionic strengths from 0 to 0.35 M. In making calculations on such a system, it is convenient to specify concentrations of coenzymes like NADox and NADred because they are involved in many reactions and may be in steady states. Calculations are given for [NADox] = 1000[NADred] and [NADox] = 10[NADred]. Equilibrium compositions are calculated using computer programs when all the reactants are present initially and when only glyoxylate and CoA are present initially. The kinetics of the reactions in the glyoxylate cycle at specified concentrations of NADox and NADred are calculated by numerical solution of the steady-state rate equations for the case where the reactant concentrations are below their Michaelis constants and only glyoxylate and CoA are present initially.

Tools

SciFinder Links

SciFinder subscribers:  Click to sign in | Not a SciFinder subscriber? Learn more at www.cas.org

History

  • Published In Issue December 26, 2006
  • Received September 1, 2006
    Revised Manuscript Received October 18, 2006

Recommend & Share

Related Content

Other ACS content by these authors: