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The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo= Vmax [S] akm + a' [S] where Vo is initial velocity, Vmax is maximum velocity. [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches Vmax Apparent, or observed. Km is equivalent to the [S] at which V= Vmax 2a Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. V apparent Km max al Incorrect 0 -1

The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo= Vmax [S] akm + a' [S] where Vo is initial velocity, Vmax is maximum velocity. [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches Vmax Apparent, or observed. Km is equivalent to the [S] at which V= Vmax 2a Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. V apparent Km max al Incorrect 0 -1

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo= Vmax [S] akm + a' [S] where Vo is initial velocity, Vmax is maximum velocity. [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches Vmax Apparent, or observed. Km is equivalent to the [S] at which V= Vmax 2a Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. V apparent Km max al Incorrect 0 -1
Transcribed Image Text:The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo= Vmax [S] akm + a' [S] where Vo is initial velocity, Vmax is maximum velocity. [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches Vmax Apparent, or observed. Km is equivalent to the [S] at which V= Vmax 2a Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. V apparent Km max al Incorrect 0 -1
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