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Enzyme Kinetics at High Enzyme Concentration

✍ Scribed by S. Schnell; P.K. Maini


Book ID
102566550
Publisher
Springer
Year
2000
Tongue
English
Weight
222 KB
Volume
62
Category
Article
ISSN
1522-9602

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✦ Synopsis


We re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with the aid of the reverse quasi-steady-state assumption, we challenge the approximation d[C]/dt β‰ˆ 0 for the basic enzyme reaction at high enzyme concentration. For the first time, an approximate solution for the concentrations of the reactants uniformly valid in time is reported. Numerical simulations are presented to verify this solution. We show that an analytical approximation can be found for the reactants for each initial condition using the appropriate quasi-steady-state assumption. An advantage of the present formalism is that it provides a new procedure for fitting experimental data to determine reaction constants. Finally, a new necessary criterion is found that ensures the validity of the reverse quasi-steady-state assumption. This is verified numerically.


πŸ“œ SIMILAR VOLUMES


Michaelis-Menten kinetics at high enzyme
✍ A.R. Tzafriri πŸ“‚ Article πŸ“… 2003 πŸ› Springer 🌐 English βš– 266 KB

The total quasi-steady state approximation (tQSSA) for the irreversible Michaelis-Menten scheme is derived in a consistent manner. It is found that self-consistency of the initial transient guarantees the uniform validity of the tQSSA, but does not guarantee the validity of the linearization in the

Enzyme Kinetics
✍ HAMMOND, B. R. πŸ“‚ Article πŸ“… 1958 πŸ› Nature Publishing Group 🌐 English βš– 126 KB