In the double-reciprocal plot, increasing the concentration of inhibitorA. 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.

Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…

Answered: In the double-reciprocal plot,…

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 V_max.

B. lowers the K_m / V_max.

C. raises the K_m / V_max.

D. lowers the K_m.

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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