Noncompetitive Inhibitors You can think of noncompetitive inhibition as a combination of both competitive and uncompetitive inhibition. Noncompetitive inhibitors interact with both the free enzyme and the enzyme substrate complex and has the same affinity for both. Show how the addition of a noncompetitive inhibitor would affect the reaction velocity and double-reciprocal plots shown below. Reaction velocity (Vo)→ Vmax Vmax/2 KM Va Substrate concentration [S] max 1/Vo Slope=KM/Vmax Z Intercept = 1/Vmax Intercept = -1/KM 0 1/[S]
Noncompetitive Inhibitors You can think of noncompetitive inhibition as a combination of both competitive and uncompetitive inhibition. Noncompetitive inhibitors interact with both the free enzyme and the enzyme substrate complex and has the same affinity for both. Show how the addition of a noncompetitive inhibitor would affect the reaction velocity and double-reciprocal plots shown below. Reaction velocity (Vo)→ Vmax Vmax/2 KM Va Substrate concentration [S] max 1/Vo Slope=KM/Vmax Z Intercept = 1/Vmax Intercept = -1/KM 0 1/[S]
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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![**C. Noncompetitive Inhibitors**
Noncompetitive inhibition can be understood as a combination of both competitive and uncompetitive inhibition. Noncompetitive inhibitors interact with both the free enzyme and the enzyme-substrate complex, having the same affinity for both.
The following plots illustrate how the addition of a noncompetitive inhibitor affects reaction velocity and double-reciprocal plots.
**First Graph:**
- The Y-axis represents the reaction velocity (V₀).
- The X-axis represents the substrate concentration [S].
- The curve shows that with increasing substrate concentration, the reaction velocity approaches a maximum velocity (Vmax).
- The point where the curve reaches half of Vmax represents the Michaelis constant (KM).
**Second Graph (Double-Reciprocal Plot):**
- This is a Lineweaver-Burk plot.
- The Y-axis is 1/V₀ (inverse of reaction velocity).
- The X-axis is 1/[S] (inverse of substrate concentration).
- The slope of the line is KM/Vmax.
- The Y-intercept is 1/Vmax.
- The X-intercept is -1/KM.
Noncompetitive inhibitors decrease the overall reaction rate without affecting the affinity (KM) of the enzyme for the substrate.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F321fd000-515a-4cf5-ac03-99096af58e6a%2F43d422a2-b1fb-4773-9993-0eac57cee57b%2Fwi5m3kk_processed.jpeg&w=3840&q=75)
Transcribed Image Text:**C. Noncompetitive Inhibitors**
Noncompetitive inhibition can be understood as a combination of both competitive and uncompetitive inhibition. Noncompetitive inhibitors interact with both the free enzyme and the enzyme-substrate complex, having the same affinity for both.
The following plots illustrate how the addition of a noncompetitive inhibitor affects reaction velocity and double-reciprocal plots.
**First Graph:**
- The Y-axis represents the reaction velocity (V₀).
- The X-axis represents the substrate concentration [S].
- The curve shows that with increasing substrate concentration, the reaction velocity approaches a maximum velocity (Vmax).
- The point where the curve reaches half of Vmax represents the Michaelis constant (KM).
**Second Graph (Double-Reciprocal Plot):**
- This is a Lineweaver-Burk plot.
- The Y-axis is 1/V₀ (inverse of reaction velocity).
- The X-axis is 1/[S] (inverse of substrate concentration).
- The slope of the line is KM/Vmax.
- The Y-intercept is 1/Vmax.
- The X-intercept is -1/KM.
Noncompetitive inhibitors decrease the overall reaction rate without affecting the affinity (KM) of the enzyme for the substrate.
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