Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations
β Scribed by S. Schnell; P.K. Maini
- Publisher
- Elsevier Science
- Year
- 2002
- Tongue
- English
- Weight
- 532 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0895-7177
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β¦ Synopsis
Analytic
approximations of the time-evolution of the single enzyme-substrate reaction are valid for all but a small region of parameter spsce in the positive initial enzyme-initial substrate concentration plane. We find velocity equations for the substrate decomposition and product formation with the aid of the total quasi-steady-state approximation and an aggregation technique for cases where neither the more normally employed standard nor reverse quasi-steady-state approximations are valid. Applications to determining reaction kinetic parameters are discussed.
π SIMILAR VOLUMES
Expressions are derived for the parameters that can be obtained from (1) steady-state kinetics, (2) isotope-exchange kinetics at equilibrium, and (3) equilibrium binding experiments for the following two one-substrateone-product enzymic mechanisms: It is shown that the exchange constants for both m
A special mixing device for initiating enzyme-catalyzed reactions is used to rapidly achieve an unperturbed quasi-steady state. An on-line computer is employed to sample the initial conditions, the mixing time, and concentrations that change as a function of time during this quasi-steady state phase