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.
Choose the plot that best reflects the activity of an enzyme inhibited irreversibly. 100% A C D time A D C B Enzyme Activity
5. By using Excel or GoogleSheets. graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Kwax values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive? [S] (mM) V, No Inhibitor (mmol min-) V, Inhibitor Present (mmol min-') 1 × 10-4 5 × 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 0.026 0.010 0.092 0.136 0.040 0.086 0.150 0.120 0.165 0.142
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.
D 1. 0.25 Short answer questions, write answers on blank paper. A plot of enzyme activity with and without an inhibitor present gave the following plot. 0.2 0.15 1/V v in mM/s 0.1 0.05 0 0 0.05 0.1 y=0.67x+0.02 0.15 y=0.2x+0.02 0.2 0.25 0.3 1/[S]. [S] in mM Without the inhibitor, what are the values of Vmax and Km? In the presence of the inhibitor, which of these items has changed and what is (are) the new value(s)? What type of inhibitor is present (explain why you have arrived at this conclusion)? Be sure to include units as necessary--answers that do not contain required units will be marked incorrect
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.
When k2 >> k-1, KM approximates the affinity of the enzyme•substrate complex.The (circle one) higher / lower the KM, the more tightly the enzyme binds to its substrate
A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme 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