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Steady State Enzyme Velocities That Are Independent of [Enzyme]:  An Important Behavior in Many Membrane and Particle-Bound States

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Department of Biochemistry, University of Minnesota, St. Paul, Minnesota 55108
Cite this: Biochemistry 1997, 36, 30, 9081–9086
Publication Date (Web):July 29, 1997
Copyright © 1997 American Chemical Society

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    The popular paradigm for biological education in kinetics involves descriptions that are appropriate for soluble enzymes. Derivations seldom present the assumptions on which the fundamental parameter of these kinetics, the site rate constant, is based. This omission can create difficulty for understanding situations where the assumptions are invalid. Membrane- and particle-bound enzyme systems provide several examples. In fact, biological organisms show macroscopic design and enzyme expression levels which suggest utilization of alternative kinetic mechanisms. The role of substrate affinity and enzyme inhibitors is greatly altered, with correlated impact on biomedical and biotechnological designs. Enzymes may perform functions such as isolation of cell contents from the environment, an action that is usually reserved for membranes. These properties can be mimicked but never perfectly replicated in purified systems. This presentation provides a description of some of these behaviors for membrane- or particle-bound enzymes, using an approach that is closely correlated with the manner in which steady state enzyme kinetics are typically presented.

     Supported in part by Grant HL15728 and GM38819 from the National Institutes of Health.


     Corresponding author:  Department of Biochemistry, 1479 Gortner Ave., St. Paul, MN 55108. Fax:  (612) 625-5780. E-mail:  [email protected]. Phone:  (612) 624-3622.

     Abstract published in Advance ACS Abstracts, July 15, 1997.

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