Control Analysis of Systems with Enzyme-Enzyme Interactions

  • Henrik Kacser
  • Herbert M. Sauro
  • Luis Acerenza
Chapter
Part of the NATO ASI Series book series (NSSA, volume 190)

Abstract

The classical approach to control analysis has made two fundamental assumptions: the first is that all enzymes are independently acting catalysts, and the second is that the reaction rate of an isolated enzyme is first-order with respect to enzyme concentration. The first assumption, that of independence, implies that no direct interactions between enzymes affect their catalytic activities (other than that which occurs indirectly through the common substrate or effector pools). This assumption would be invalid, for example, if dynamic enzyme-complex formation affected the kinetic parameters of the constituent enzymes. The second assumption, that of additivity, based on classical enzymology, would not apply if, for example, an enzyme oligomer-monomer equilibrium existed for a single reaction step, or if the enzyme were partitioned between free and membrane-bound forms, the membrane being present in fixed amount, with different activities of the two forms.

Keywords

Enzyme Concentration Control Analysis Elasticity Coefficient Common Substrate Control Coefficient 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Henrik Kacser
    • 1
  • Herbert M. Sauro
    • 1
  • Luis Acerenza
    • 1
  1. 1.Department of GeneticsUniversity of EdinburghEdinburghUK

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