Vinnakota2006_MuscleGlycogenolysis_ModelC

This a model from the article:
Dynamics of muscle glycogenolysis modeled with pH time course computation and
pH-dependent reaction equilibria and enzyme kinetics.

Vinnakota K, Kemp ML, Kushmerick MJ. Biophys J
2006 Aug 15;91(4):1264-87 16617075
,
Abstract:

Cellular metabolites are moieties defined by their specific binding constants to
H+, Mg2+, and K+ or anions without ligands. As a consequence, every biochemical
reaction in the cytoplasm has an associated proton stoichiometry that is
generally noninteger- and pH-dependent. Therefore, with metabolic flux, pH is
altered in a medium with finite buffer capacity. Apparent equilibrium constants
and maximum enzyme velocities, which are functions of pH, are also altered. We
augmented an earlier mathematical model of skeletal muscle glycogenolysis with
pH-dependent enzyme kinetics and reaction equilibria to compute the time course
of pH changes. Analysis shows that kinetics and final equilibrium states of the
closed system are highly constrained by the pH-dependent parameters. This
kinetic model of glycogenolysis, coupled to creatine kinase and adenylate
kinase, simulated published experiments made with a cell-free enzyme mixture to
reconstitute the network and to synthesize PCr and lactate in vitro. Using the
enzyme kinetic and thermodynamic data in the literature, the simulations
required minimal adjustments of parameters to describe the data. These results
show that incorporation of appropriate physical chemistry of the reactions with
accurate kinetic modeling gives a reasonable simulation of experimental data and
is necessary for a physically correct representation of the metabolic network.
The approach is general for modeling metabolic networks beyond the specific
pathway and conditions presented here.
This model was taken from the CellML repository
and automatically converted to SBML.
The original model was:
Vinnakota K, Kemp ML, Kushmerick MJ. (2006) - version=1.0

The original CellML model was created by:
Geoffrey Nunns

[e-mail]
The University of Auckland
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