Indicate how the observed Km of an enzyme would change in the presence of inhibitors having the given effect on a and a'.IncreasedDecreasedUnchangedAnswer Banka = a'α>α'a' > aa = a' := 1.0a' > 1.0a' = 1.0

The Km is known as Michaelis constant, it is the concentration of substrate at which reaction…

Answered: indicate how the observed Km of an…

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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The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (uM) 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Km of the inhibited enzyme reaction?
you are trying to come up with a drug to inhibit the activity of an enzyme thuogth to have a role in a liver disease. in the lab the enzyme was shown to have a Km of 1x10-6 M and Vmax of 0.1 micromoles/min.mg measruing at room temperature. you developed a mixed non-competitve inhibitor with a ki=0.4x10-6M and a Ki` pf 0/2 x 10-5 What will be the apparent Km in the presence of 1.0x10-6 M?
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.
1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
From the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.
Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.
5.50 1/V, min/umol 5.00 4.50 4.00 y = 0.9474x + 2.6649 y = 0.9997x + 2.032 0.00 1.00 2.00 2.50 3.00 1/[S], uM -1 Looking at the double reciprocal plot for an enzyme in the absence of inhibitor and in the presence of two concentrations of inhibitor, what would be the Vmax for the uninhibited enzyme? (bottom graph) Equation is given. Choose the one best answer. 3.50 3.00 2.50 2.00
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.
Draw Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Vmax values for the inhibited and uninhibited rxns? Is the inhibitor competitive or noncompetitive? [S] (M) 10,000 1 x 104 2.000-5 x 104 666673 1.5 x 10-3 400- 2.5 x 10-³ 2005x103 V, No Inhibitor (Arbitrary units) 0.026 38,461 0.092 10.87 37100 0.136 7.35 Wak 0.150 -67 0.165 6.06 L slope: 0033 yint=5057 полесте um.x=0.198 km 6.5x 10-4 0.010 0.040 25 10.086 11.63 0.120 8.33 0.142 7.04 2500 V, Inhibitor Present (Arbitrary Units) 100 ↓ $op.= .009 yint: 5.21 900x12 km: 1.73 y/o conf. V10-3 321000
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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indicate how the observed Km of an enzyme would change in the presence of inhibitors having the given effect on a and a'. Increased Decreased Unchanged Answer Bank a = a' a > a' a' > a a = a' = 1.0 a' > 1.0 a' = 1.0