Curien2009_Aspartate_Metabolism

This a model described in the article:
Understanding the regulation of aspartate metabolism using a model based on measured kinetic parameters.

Curien G, Bastien O, Robert-Genthon M, Cornish-Bowden A, Cárdenas ML, Dumas R. Mol Syst Biol.
2009;5:271. Epub 2009 May 19. PMID: 19455135
, doi: 10.1038/msb.2009.29

Abstract:

The aspartate-derived amino-acid pathway from plants is well suited for analysing the function of the allosteric network of interactions in branched pathways. For this purpose, a detailed kinetic model of the system in the plant model Arabidopsis was constructed on the basis of in vitro kinetic measurements. The data, assembled into a mathematical model, reproduce in vivo measurements and also provide non-intuitive predictions. A crucial result is the identification of allosteric interactions whose function is not to couple demand and supply but to maintain a high independence between fluxes in competing pathways. In addition, the model shows that enzyme isoforms are not functionally redundant, because they contribute unequally to the flux and its regulation. Another result is the identification of the threonine concentration as the most sensitive variable in the system, suggesting a regulatory role for threonine at a higher level of integration.
The limiting rates for the tRNA synthetase reactions, V_Lys_RS, V_Thr_RS and V_Ile_RS, are all assigned a joined value, Vmax_AA_RS, to facilitate reproduction of the results in the publication. To alter these rates seperately these assignments have to be changed or removed.
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