The total quasi-steady-state approximation is valid for reversible enzyme kinetics |
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Authors: | Tzafriri A R Edelman E R |
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Affiliation: | Harvard-MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology, Room 16-343, Cambridge, MA 02139, USA. ramitz@mit.edu |
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Abstract: | The Briggs-Haldane approximation of the irreversible Michaelis-Menten scheme of enzyme kinetics is cited in virtually every biochemistry textbook and is widely considered the classic example of a quasi-steady-state approximation. Though of similar importance, the reversible Michaelis-Menten scheme is not as well characterized. This is a serious limitation since even enzymatic reactions that go to completion may be reversible. The current work derives a total quasi-steady-state approximation (tQSSA) for the reversible Michaelis-Menten and delineates its validity domain. The tQSSA allows the derivation of uniformly valid approximations for the limit of low enzyme concentrations, ET
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Keywords: | Enzyme kinetics Quasi-steady-state approximation |
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