Q16: The graph shows three plots of velocity (vo) versus substrate concentration ([S]). Determine which curve represents an enzyme'sreaction velocity without any inhibitor present, which curve represents the velocity in the presence of a noncompetitiveinhibitor, and which curve represents the velocity in the presence of a competitive inhibitor.maxVmaxVoSelect all of the true statements.[S] (₂M)Answer Bankcompetitive inhibitorno inhibitornoncompetitive inhibitorA higher substrate concentration is associated with a faster reaction rate if the enzyme is not saturated.A competitive inhibitor decreases the maximum rate at which a reaction can proceed.When substrate is present in excess, the maximum reaction rate is unchanged in the presence of a competitive inhibitor.

Enzymes are biological catalysts that increase rate of biochemical reactions.Most enzymes are…

Answered: The graph shows three plots of velocity…

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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What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is impact of the lower V max on the amount of product formed ? If the lower value of black resulting in the new plot (red curve) is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible ? And why?
The figure below shows the dependence of the enzyme's rate, v (in µM/min), as a function of substrate concentration, S (in mM). Also shown is the dependence of the rate in the presence of an inhibitor, present at a concentration of 0.2 mM. Based on this information, which of the following does this inhibitor most likely interact with? 1/v 1- 05 1/[S) O A. Michaelis complex O B. [E O C. free enzyme O D. free substrate O E. Both "A" and "B."
The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo = Vmax [S] aKm + a' [S] where Vis 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 Vmax 2a' Apparent, or observed, Km is equivalent to the [S] at which Vo = 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. apparent Km =
A plot of 1/Vo versus 1/[S], called Lineweaver-Burk or double-reciprocal plot, is a useful tool for identifying the type of enzyme inhibition. What is the type of inhibition indicated by the graph? with inhibitor MS) OA Uncompetitive inhibition OB. Competitive inhibition The type of inhibition cannot be determined from the graph provided. OC. O D. Noncompetitive inhibtion
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/Vm Vmax 2α' 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. = Apparent, or observed, Km is equivalent to the [S] at which Vo max. apparent Km =
Explain how the following changes affect the rate of an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor: (a) increasing the substrate concentration at a constant inhibitor concentration, (b) decreasing the inhibitor concentration at a constant substrate concentration.
A с Wan WWW GHEDE MAK am2 Increasing CE a-1 (no inhibitor) Slope #KY... ...." 7-15 7 a>c²=1 [no inhibitori Slope R 101 9-19 aver-Burk plots in this figure represent the activities of enzymes in the 4-5 n. 155 B D MIN -a'/KM 0.8- 1/V >~- -1/K 0 01 m(app) d'Nmax a=2 a=1.5 1[S] per mM inhibitor a=10 Slope K
What enzyme kinetic parameters are apparently impacted by competitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor Vmax
A medicinal chemist is trying to determine the mechanism of action of inhibitors she has synthesized. The relative change in KM and Vmax upon incubation of the targeted enzyme with each inhibitor is shown in the table below. Inhibitor A Inhibitor B Inhibitor C Using this data, the mechanism of action of Inhibitor C is: Uncompetitive TS‡ analog Mixed Inhibition Competitive Кмарр- Км 0 Non-competitive app - Vmax <0 <0 0 Vmax
Write Cifonly statement A is correct, Hif only statement B is correct, Eif both statements are correct, Mif both statements are incorrect. A. When an inhibitor binds to the enzyme-substrate complex, the inhibition mode is uncompetitive. B. As a consequence, the enzyme's efficiency is decreased along with the maximum velocity.
For the competitive, noncompetitive and uncompetitive inhibition type investigate following figures and determine relationship between inhibitor concentration and Vmax and Km for each mechanism.
The graphs 3 and 4 representing 1/Vo = f(1/[S]o) have been done in the presence of a competitive (CI) and noncompetitive inhibitor (NCI). a- For each figure, determine from the relative position of the straight lines which one is obtained in presence of an inhibitor. b- Indicate which graph corresponds to the competitive inhibition and which one the noncompetitive inhibition. Justify your answer. c- Complete the graphs by indicating which values can be determined from the arrows. 3 1/No 1/[S]⁰ (4) 1/No 1/[S]o

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