Four sequential, first-order enzymatic reactions S <--> P with substrates binding to enzymes, and reversible product formation.
Model number: 0275
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Figure: Shows the rapid equilibration which was assumed by Michaelis and Menten for their reaction kinetic approximation to be valid. This results in the reaction from ES complex to product P being the rate limiting step in the process. Under the conditions set, with Kp >> Kd the reaction is almost irreversible resulting in progressive appearance of the products with almost no effective reversibility. (Kp is the equilibrium dissociation constant for P binding to E and Kd is the equilibrium dissociation constant for substrate S binding to E). Top figure shows the amount of substrate available at each enzymatic reaction step. Bottom figure shows the relative amount of enzyme bound to substrate for each reaction as a function of time.
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Bassingthwaighte JB.: Enzymes and Metabolic Reactions, Chapter 10 in "Transport and Reactions in Biological Systems", Pages 7-8
- Go to Compartmental tutorial overview.
- Enzymatic reactions in series.
- One reversible enzymatic reaction.
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[This page was last modified 29Jan20, 1:02 pm.]
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