Enzyme systems within living cells have recently been shown to be highly ordered structures that violate classic assumptions of the Michaelis-Menten formalism, which originally was developed for the characterization of isolated reactions in vitro. This evidence suggests that a thorough examination of alternative kinetic formalisms for integrated biochemical systems is in order. The purpose of this series of papers is to assess the utility of an alternative power-law formalism by carrying out a detailed comparative analysis of a relatively large, representative system - the tricarboxylic acid cycle of Dictyostelium discoideum. This system was chosen because considerable experimental information already has been synthesized into a detailed kinetic model of the intact system. In this first paper, we set the stage for subsequent analysis within the framework of the power-law formalism: we review the underlying theory, emphasizing recent developments, formulate the model in terms that are convenient for the analysis to follow, and develop the system representation in both the Michaelis-Menten and power-law forms. In the second paper (Shiraishi, F., and Savageau, M. A. (1992) J. Biol. Chem. 267, 22919-22925), these alternative representations are shown to be internally consistent and locally equivalent. The third paper (Shiraishi, F., and Savageau, M. A. (1992) J. Biol. Chem. 267, 22926-22933) provides a complete analysis of the steady state behavior and also treats the dynamic behavior of the model.
|Original language||English (US)|
|Number of pages||7|
|Journal||Journal of Biological Chemistry|
|State||Published - Nov 15 1992|
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