no inhibitorinhibitor Ainhibitor BVV = velocity (rąte)[S] = substrate concentration[S]Copy the graphs,Label the graph for 'no inhibitor' to show the position of V, ½V andmaxmaxamb State the effect that inhibitor A had on V and K of the enzyme.of the enzyme.maxand KmState the effect that inhibitor B had on Vmaxd Which inhibitor is competitive and which is non-competitive?Explain your answer.Total 12 Two inhibitors of the same enzyme, inhibitor A and inhibitor B, wereinvestigated to discover if they were competitive or non-order to do this, the rate of reaction of the enzyme was measured at differentconcentrations of substrate without inhibitor, with inhibitor A and withinhibitor B. Graphs of the data were plotted as shown. The graphs showedthat one inhibitor was competitive and the other non-competitive.on-competitive. In

Enzyme catalysis a reaction where substrate is converted into product with a minimal activation…

Answered: Label the graph for 'no inhibitor' to…

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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A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown below: [Substrate] (mM) Vo (mM/min) (without inhibitor) Vo (mM/min) (with inhibitor) 15 1.11 0.67 30 1.81 1.17 45 2.28 1.56 60 2.62 1.88 90 3.09 2.36 Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the absence of an inhibitor. y-int [ Select ] slope [ Select] • Vmax (Sclect] mM/min Km [ Sclect) mM
The Km value of an enzyme is affected in the presence of a competitive inhibitor because it requires more substrate to achieve the same Vmax as without the inhibitor. True False
The Lineweaver-Burke plots of a reaction without inhibitor and one with non-competitive inhibitor will have the same 1. Vmax2. Km3. Km/Vmax4. 1/Vmax
Which statements are true of an inhibitor that binds the active site of an enzyme? Select all that apply, there may be one correct answer or several. a These inhibitors are a kind of allosteric regulator that decreases enzyme activity. b Adding more substrate can reduce the effect of these inhibitors. c These inhibitors compete with the substrate for the active site of the enzyme. d These inhibitors increase the rate of enzyme activity. e These inhibitors function by changing the shape of the enzyme, stopping if from binding to substrate.
The 2 eynzymes are affected by a substrate. Choose all correct answers.
kcat is: a measure of the catalytic efficiency of the enzyme the rate constant for the reaction ES → E + P the rate constant for the reaction ES → E + S the [S] that half saturates the enzyme ½ Vmax
(a) You are given the following experimental measurements for the effects of an inhibitor on the initial velocity of an enzymatic reaction. Plot the data and determine what type of inhibition is being observed. Label all axes. [S] (MM) Vo (mM • Vo with I present (mM ⚫s-¹) 1 2.8 3 6.0 1.0 2.5 4 7.0 3.1 8 9.9 12 11.5 4.8 5.7 (b) Briefly explain how varying [S] can be used to determine whether an inhibitor is uncompetitive or competitive. Be sure to include in your explanation why this method would work.
From the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.
Graph a double reciprocal plot that satisfy the following: a. Michaelis-Menten kinetics enzyme, b. an inhibitor that binds only free enzyme (competitive), c. an inhibitor that binds only enzyme-substrate complex.
A newly developed drug is suspected to act by inhibiting its enzymatic target. To test this, the rates of reaction in the presence and absence of the new drug were determined. The results of these experiments have been plotted as a double reciprocal plot shown in figure 1 below. Using this figure, calculate the values of Vmax and Km for the enzyme in the presence and absence of the drug. 2. Based on the figure and your answer, what type of inhibition is the new drug displaying? 3. Briefly explain how this type of inhibition exerts its action on an enzyme. Figure 1: Double reciprocal plot of reaction rate against substrate concentration in the presence and absence of a new drug.
In Lineweaver Burk plot: O a. The slope of the plot is the Vmax/Km O b. The intercept on X-axis is 1/Km. O c. The intercept on y-axis is 1/Vmax O d. double-reciprocal plot of enzyme kinetics is generated, where 1/VO is plotted as a function [S]. O e. All answers are correct
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."

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Label the graph for 'no inhibitor' to show the position of V,½V K State the effect that inhibitor A had on V and K State the effect that inhibitor B had on V and K of the enzyme. max and max m of the enzyme. max max