Mathematical modelling of dynamics and control in metabolic networks. III. Linear reaction sequences

https://doi.org/10.1016/S0022-5193(85)80226-5Get rights and content

Kinetics of linear sequences of enzymatic reactions converting a single substrate into a single product are examined with emphasis on obtaining the relationship between the individual kinetic parameters and overall dynamic behavior. Chains of reactions exhibiting irreversible Michaelis-Menten kinetics are examined via scaling, linearization and modal analysis. The modal analysis gives the conditions under which the quasi-steady state assumption is applicable for one reaction relative to another in such a reaction sequence. The linearized description permits characterization of the transient response in terms of temporal moments. The moments provide useful physical insight and also provide a basis for systematic model reduction.

References (19)

  • DarveyI.G. et al.

    Bull. math. Biol.

    (1978)
  • GibilaroL.G. et al.

    Chem. Eng. Sci.

    (1969)
  • HammesG.G. et al.
  • HommesF.A.

    Arch. Biochem. Biophys.

    (1962)
  • PalssonB.O. et al.

    J. theor. Biol.

    (1984)
  • PalssonB.O. et al.

    J. theor. Biol.

    (1984)
  • ParkD.J.M.

    J. theor. Biol.

    (1974)
  • SrereP.A.

    Biochem. Med.

    (1970)
  • AtkinsonD.E.

    Cellular Energy Metabolism and its Regulation

    (1977)
There are more references available in the full text version of this article.

Cited by (25)

  • How growth affects the fate of cellular metabolites

    2005, Bulletin of Mathematical Biology
View all citing articles on Scopus

Present address: Department of Chemical Engineering, Dow Building, University of Michigan, Ann Arbor, Michigan 48109, U.S.A.

§

Present address: Mẏndamȯt HF, Bolholt 6, Reykjavik, Iceland.

View full text