You are studying an enzyme and wish to determine how an inhibitor functions. The enzyme reaction is A->P. You perform two experiments, one measuring enzyme activity without inhibitor and one measuring enzyme activity with 200 uM inhibitor. The results are presented below: No inhibitor a (uM) v (uM/sec) 10 15 25 40 70 8.333 10.714 13.889 16.667 19.444 200 uM inhibitor a (UM) v (uM/sec) 10 15 25 40 70 6.250 7.500 8.929 10.000 10.938 What are Vmax, KM, K₁. What type of inhibition does I cause?

You are studying an enzyme and wish to determine how an inhibitor functions. The enzyme reaction is A->P. You perform two experiments, one measuring enzyme activity without inhibitor and one measuring enzyme activity with 200 uM inhibitor. The results are presented below: No inhibitor a (uM) v (uM/sec) 10 15 25 40 70 8.333 10.714 13.889 16.667 19.444 200 uM inhibitor a (UM) v (uM/sec) 10 15 25 40 70 6.250 7.500 8.929 10.000 10.938 What are Vmax, KM, K₁. What type of inhibition does I cause?

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

See similar textbooks

Similar questions

In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor. In each batch, the inhibitor was of a different type: a.Batch 1: competitive inhibitor b.Batch 2:uncompetitive inhibitor c.Batch 3:non-competitive inhibitor Assuming that Vmax = 80 mM s', Km = 8 mM, and Kiof all three inhibitors was 10 mM, which of the inhibitors was the most efficient on Vo? Explain your answer.
(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.
Using the table below can you please help me answer the following. Based on your results, what can you conclude about the effect of enzyme concentration on reaction rate? Explain
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 potent inhibitor effectively inhibits an enzyme catalyzed reaction. What kind of a Ki value you would expect for a potent inhibitor?
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.
You run a series of assays at 25°C on enzyme A. You measure the velocity for a range of S concentrations. What is the Km (in mM) for Enzyme A?
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."
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.
What is the relative inhibition of an enzyme by a competitive inhibitor at [S] = KS and [I] = KI?
Why is it important to know the Km and Vmax values of an enzyme?
Calculate 1/[S] and 1/V to complete the table. Use this data to draw a Lineweaver-Burke plot, with lines for ‘no inhibitor’ and ‘with inhibitor’. Be sure to label your axes and lines. What kind of inhibitor is it? Estimate Vmax and Km for the uninhibited reaction.