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 con
โฆ LIBER โฆ
Micellar hydrolysis of hydroxamic acids. Michaelis-menten kinetics
โ Scribed by Donald C. Berndt; Jill E. Angus; Michael J. Wood; Richard F. Atkinson; Tanveer A. Qureshi; Brian J. Shay; Aura I. Provancher
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 364 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0538-8066
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โฆ Synopsis
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-methylhydroxamic acids exhibited only first-order kinetics. The results are consistent with the Michaelis-Menten rate equation.
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