In the double-reciprocal plot, increasing the concentration of inhibitor A. raises the Vmax. B. lowers the Km / Vmax. C. raises the Km / Vmax. D. lowers the Km.
In the double-reciprocal plot, increasing the concentration of inhibitor A. raises the Vmax. B. lowers the Km / Vmax. C. raises the Km / Vmax. D. lowers the Km.
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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Question
In the double-reciprocal plot, increasing the concentration of inhibitor
A. raises the Vmax.
B. lowers the Km / Vmax.
C. raises the Km / Vmax.
D. lowers the Km.
![This image is a graphical representation of enzyme kinetics, specifically a Lineweaver-Burk plot, which is used to illustrate the effect of inhibitors on enzymatic reactions.
**Lineweaver-Burk Plot:**
Axes:
- The x-axis is labeled as "1/[S]", where [S] is the substrate concentration.
- The y-axis is labeled as "1/v", where v is the reaction velocity.
Lines:
- Three lines are shown, all of which intersect at a common point on the y-axis but diverge in their slopes.
- The bottom line is labeled as "No inhibitor," indicating that it represents enzyme kinetics without any inhibitors present.
- Two additional lines above the "No inhibitor" line are labeled "Increasing inhibitor," representing the presence of increasing concentrations of an inhibitor in the enzymatic reaction.
Explanation:
- The plot exhibits how the presence of inhibitors affects the enzyme's activity. Without inhibitors, the reaction follows the expected kinetics (as shown by the "No inhibitor" line).
- With the increasing presence of inhibitors, the slope of the line increases, demonstrating that the reaction rate decreases more significantly as substrate concentration is increased.
- The different lines' intercepts on the y-axis suggest that as the inhibitor concentration increases, the maximum possible reaction rate (\(V_{max}\)) decreases and/or the apparent affinity of the enzyme for the substrate (reflected in \(1/K_M\)) is altered.
This visual tool is essential in understanding how inhibitors influence enzyme kinetics and thus is frequently used in biochemical studies to characterize the type and efficacy of enzyme inhibitors.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F0b314f3d-0016-4e6e-b543-d69b758dc3e8%2F805b102d-9c02-42b4-aae6-faa48f8a3448%2F56gpjvl_processed.png&w=3840&q=75)
Transcribed Image Text:This image is a graphical representation of enzyme kinetics, specifically a Lineweaver-Burk plot, which is used to illustrate the effect of inhibitors on enzymatic reactions.
**Lineweaver-Burk Plot:**
Axes:
- The x-axis is labeled as "1/[S]", where [S] is the substrate concentration.
- The y-axis is labeled as "1/v", where v is the reaction velocity.
Lines:
- Three lines are shown, all of which intersect at a common point on the y-axis but diverge in their slopes.
- The bottom line is labeled as "No inhibitor," indicating that it represents enzyme kinetics without any inhibitors present.
- Two additional lines above the "No inhibitor" line are labeled "Increasing inhibitor," representing the presence of increasing concentrations of an inhibitor in the enzymatic reaction.
Explanation:
- The plot exhibits how the presence of inhibitors affects the enzyme's activity. Without inhibitors, the reaction follows the expected kinetics (as shown by the "No inhibitor" line).
- With the increasing presence of inhibitors, the slope of the line increases, demonstrating that the reaction rate decreases more significantly as substrate concentration is increased.
- The different lines' intercepts on the y-axis suggest that as the inhibitor concentration increases, the maximum possible reaction rate (\(V_{max}\)) decreases and/or the apparent affinity of the enzyme for the substrate (reflected in \(1/K_M\)) is altered.
This visual tool is essential in understanding how inhibitors influence enzyme kinetics and thus is frequently used in biochemical studies to characterize the type and efficacy of enzyme inhibitors.
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