alexa Enzyme Catalysis and the Outcome of Biochemical Reactions

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Enzyme Catalysis and the Outcome of Biochemical Reactions

The investigation of enzyme catalysis has traditionally been based on the rapid equilibrium conditions defined by Henri, Michaelis and Menten. The general rate equations derived by Briggs and Haldane provided incremental progress by assuming near steady-state levels for the enzyme-substrate complex. In situ, however, enzymes may operate far from equilibrium, so that the idealizing assumptions of traditional enzyme kinetics do not hold up and the enzyme becomes an active participant in determining the outcome of a reaction. We used computer modeling of an enzyme-catalyzed reaction with substrate activation to assess the impact of the rate constants on the product production per unit time. Mapping of the parameter space in bifurcation plots displayed ranges of instability that were preceded and succeeded by distinct stable states.

Citation: Milanowski P, Carter TJ, Weber GF (2013) Enzyme Catalysis and the Outcome of Biochemical Reactions. J Proteomics Bioinform 6:132-141. doi: 10.4172/jpb.1000271

 
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