Multiple Intermediates in Steady-state Enzyme Kinetics. IV. The Steady State Kinetics of Isotopic Exchange in Enzyme-catalyzed Reactions
โ Scribed by Alberty, Robert A.; Bloomfield, Victor.; Peller, Leonard.; King, Edward L.
- Book ID
- 125901155
- Publisher
- American Chemical Society
- Year
- 1962
- Tongue
- English
- Weight
- 473 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0002-7863
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๐ SIMILAR VOLUMES
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
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