What are the assumptions that Michaelis and Menten made to derive their equation? Under whatconditions do each of the assumptions hold true?
Added by Danny L.
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This assumption holds true when the concentration of the substrate is much higher than that of the enzyme, allowing for a significant amount of ES complex formation. Show more…
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List the assumptions of the Michaelis-Menten equation, and why the model does not work if each of those assumptions are violated.
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What are the main assumptions of the Michaelis-Menten approach to describing enzyme kinetics? Define and explain: Km, k2, k1, k-1, [ES], and Vmax.
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The Michaelis-Menten equation is one of the fundamental equations describing the way single substrate enzymes behave. This equation is often represented as the following: v = Vmax[S] / (Km + [S]) v represents the rate of the reaction catalyzed by a certain enzyme, Vmax the maximum achievable rate of the reaction, Km represents the Michaelis-Menten constant, and [S] represents the concentration of substrate. Part I (20 points): Sketch the overall profile of Reaction Rate vs. Substrate Concentration. The Reaction Rate should be normalized to the maximum reaction rate, and the substrate concentration should range from 0 to 500 mM. Let Km = 15 mM and Vmax = 1 mM/s. Part II (30 points): Answer the following questions: a. What is the relationship between the maximum rate (Vmax) and the Michaelis-Menten constant (Km)? (10 points) b. Competitive inhibitors are molecules that bind to an enzyme’s active site. Which variable in the Michaelis-Menten equation do competitive inhibitors affect? Does that variable increase or decrease? (10 points) c. Many of the enzymes in oxidative phosphorylation follow the Michaelis-Menten kinetics described above. The proton pump ATPase that generates ATP using the proton concentration gradient in the mitochondria is an example. Assume that this ATPase uses the following parameters: Km = 15 mM and Vmax = 1 as before, and that the substrate concentration of ADP is usually 500 mM and it generates a given amount of ATP. Will the generation of ATP be significantly larger with [ADP] = 1000 mM? What about [ADP] = 10 × 10^6 mM? Briefly explain your answer. (10 points)
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