A probabilistic view on steady-state enzyme reactions
โ Scribed by Alexey K. Mazur
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 637 KB
- Volume
- 148
- Category
- Article
- ISSN
- 0022-5193
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โฆ Synopsis
A new theoretical description of steady-state enzyme reactions is proposed. The description is based on the concepts of the probability theory instead of the conventional formalism of chemical kinetics. A general steady-state rate equation is obtained using a probabilistic model of the catalytic act. As a result, the classical problems of enzyme kinetics can be formulated and considered in a different aspect. It is shown that the new theory presents a clearer treatment of some commonly obscure questions, such as the steady-state establishment. The theory also gives additional possibilities in the interpretation of the experimental results of traditional methods and proposes certain new ways in experimental investigations of enzymes.
๐ SIMILAR VOLUMES
The theory of the steady-state kinetics of irreversible enzyme-catalyzed homopolpmerization and copolymerization on primers has been developed. The rate law for homopolymerization is of the Michaelis-Menten form, but the kinetic parameters depend on primer concentration. Copolymerization has been tr
An enzyme catalysing the reaction of a substrate with multiple reaction sites may display steady state kinetics described by a Michaels-Menten equation. The K m is identical for all sites considered individually and all sites together. The maximum velocity for a single site depends on the rate const