One-substrate-one-product enzymic reactions: The relationship between isotope-exchange kinetic, steady-state kinetic and equilibrium parameters
โ Scribed by I.G. Darvey
- Publisher
- Elsevier Science
- Year
- 1975
- Tongue
- English
- Weight
- 464 KB
- Volume
- 49
- Category
- Article
- ISSN
- 0022-5193
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โฆ Synopsis
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 mechanisms are identical with the reciprocals of the equilibrium parameters that can be obtained from binding experiments. Therefore, expressions relating isotope exchange constants and steady-state kinetic parameters are analogous to those relating equilibrium parameters and steady-state kinetic parameters.
The paper also presents, for mechanisms I and II, relationships between the maximum rate of isotope-exchange at equilibrium and the steady-state kinetic parameters. These relationships provide a new criterion for distinguishing experimentally between these two mechanisms.
๐ SIMILAR VOLUMES
An examination of the available data for the rate of formation of enzymesubstrate complexes shows that for enzymes possessing a sequential ordered mechanism the rate constants for the formation of the various complexes (EA, etc.) are on the average two to three orders of magnitude lower than the val
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