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Vinnakota2006_MuscleGlycogenolysis_ModelC


ABSTRACT:

This a model from the article:
Dynamics of muscle glycogenolysis modeled with pH time course computation andpH-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 toH+, Mg2+, and K+ or anions without ligands. As a consequence, every biochemicalreaction in the cytoplasm has an associated proton stoichiometry that isgenerally noninteger- and pH-dependent. Therefore, with metabolic flux, pH isaltered in a medium with finite buffer capacity. Apparent equilibrium constantsand maximum enzyme velocities, which are functions of pH, are also altered. Weaugmented an earlier mathematical model of skeletal muscle glycogenolysis withpH-dependent enzyme kinetics and reaction equilibria to compute the time courseof pH changes. Analysis shows that kinetics and final equilibrium states of theclosed system are highly constrained by the pH-dependent parameters. Thiskinetic model of glycogenolysis, coupled to creatine kinase and adenylatekinase, simulated published experiments made with a cell-free enzyme mixture toreconstitute the network and to synthesize PCr and lactate in vitro. Using theenzyme kinetic and thermodynamic data in the literature, the simulationsrequired minimal adjustments of parameters to describe the data. These resultsshow that incorporation of appropriate physical chemistry of the reactions withaccurate kinetic modeling gives a reasonable simulation of experimental data andis necessary for a physically correct representation of the metabolic network.The approach is general for modeling metabolic networks beyond the specificpathway 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
gnunns1@jhu.edu
The University of Auckland

This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2011 The BioModels.net Team.
To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not..

To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.

ORGANISM(S): Homo sapiens

SUBMITTER: Camille Laibe 

PROVIDER: MODEL1006230049 | biostudies-other |

SECONDARY ACCESSION(S): 16617075

REPOSITORIES: biostudies-other

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Publications

Dynamics of muscle glycogenolysis modeled with pH time course computation and pH-dependent reaction equilibria and enzyme kinetics.

Vinnakota Kalyan K   Kemp Melissa L ML   Kushmerick Martin J MJ  

Biophysical journal 20060414 4


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 mathemat  ...[more]

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