Rates of reaction for the alkaline hydrolysis of various hydroxamic acids in the presence of cetyltrimethylammonium bromide have been determined. Empirical reaction orders of zero, one-half, and one were found for the hydroxamic acids depending upon reaction conditions and substrate structure. N-met
Michaelis-Menten mechanism reconsidered: implications of fractal kinetics
✍ Scribed by Michael A. Savageau
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 436 KB
- Volume
- 176
- Category
- Article
- ISSN
- 0022-5193
No coin nor oath required. For personal study only.
✦ Synopsis
The Michaelis-Menten formalism assumes that the elementary steps of an enzymatic mechanism follow traditional mass-action kinetics. Recent evidence has shown that elementary bimolecular reactions under dimensionally-restricted conditions, such as those that might occur in vivo when reactions are confined to two-dimensional membranes and one-dimensional channels, do not follow traditional mass-action kinetics, but fractal kinetics. A Michaelis-Menten-like reaction operating under conditions of dimensional restriction is shown to exhibit new types of synergism and noninteger kinetic orders. These properties are likely to have an important influence on the behavior of intact biochemical systems, which is largely dependent upon the kinetic orders of the constituent biochemical reactions.
📜 SIMILAR VOLUMES
Phosphorylation-induced expression or modulation of a functional protein is a common signal in living cells. Many functional proteins are phosphorylated at multiple sites and it is frequently observed that phosphorylation at one site enhances or suppresses phosphorylation at another site. Therefore,