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Updated: Jul 3, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
New constraints between kinetic parameters explain the (Un)identifiability of enzymatic rate constants
1Department of Biochemical Engineering, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands.
Abstract:
For an enzymatic reaction the rate constants in the assumed mechanism (k(1), k(-1), etc.) sometimes can be calculated from the steady-state parameter values (V(max), K(m), etc.) and sometimes cannot. When identifiability problems occur, these are obscured by redundancy occurring among the steady-state parameters. This redundancy is only partly revealed by the known Haldane relations. We found the additional constraints between the parameters. These relations allow to predict in which situation rate constants are identifiable by steady-state kinetic methods. (c) 1996 John Wiley & Sons, Inc.
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