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Updated: Aug 19, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Transient-state kinetic approach to mechanisms of enzymatic catalysis
1Laboratory of Molecular Biochemistry, Veterans Affairs Medical Center, Department of Biochemistry, University of Kansas Medical Center, 4801 Linwood Boulevard, Kansas City, MO 64128-2226, USA. hfisher@kumc.edu
Abstract:
Transient-state kinetics by its inherent nature can potentially provide more directly observed detailed resolution of discrete events in the mechanistic time courses of enzyme-catalyzed reactions than its more widely used steady-state counterpart. The use of the transient-state approach, however, has been severely limited by the lack of any theoretically sound and applicable basis of interpreting the virtual cornucopia of time and signal-dependent phenomena that it provides. This Account describes the basic kinetic behavior of the transient state, critically examines some currently used analytic methods, discusses the application of a new and more soundly based "resolved component transient-state time-course method" to the L-glutamate-dehydrogenase reaction, and establishes new approaches for the analysis of both single- and multiple-step substituted transient-state kinetic isotope effects.
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