2. An enzyme-catalyzed reaction is carried out at several different substrate concentrations (listed below), either (1) with no inhibitor, or (2) in the presence of an inhibitor, I, at 0.63 g/L. Given the following data, determine: A. what type of inhibitor I is B. the value of K₁ No Inhibitor: With Inhibitor: Substrate Concentration (g/L) 0.86 2.35 3.80 4.90 6.10 18.4 Reaction Velocity (g/L-s) 0.179 0.398 0.567 0.666 0.726 0.950 0.322 0.407 0.443 0.495 0.639 Reaction Velocity (g/L-s) 0.161

2. An enzyme-catalyzed reaction is carried out at several different substrate concentrations (listed below), either (1) with no inhibitor, or (2) in the presence of an inhibitor, I, at 0.63 g/L. Given the following data, determine: A. what type of inhibitor I is B. the value of K₁ No Inhibitor: With Inhibitor: Substrate Concentration (g/L) 0.86 2.35 3.80 4.90 6.10 18.4 Reaction Velocity (g/L-s) 0.179 0.398 0.567 0.666 0.726 0.950 0.322 0.407 0.443 0.495 0.639 Reaction Velocity (g/L-s) 0.161

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 9TYK: Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric...

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Similar questions

1. A. Estimate from the graph what the Vmax is for the enzyme without inhibitor present (black circles) and in the presence of the inhibitor (green squares). B. Estimate the Km from the graph without inhibitor present (black circles) and in the presence of the inhibitor (green squares). C. Based on the data, what type of reversible inhibitor do you think was used? 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?
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1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in eachreaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 µM. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? c. Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and KM for the enzyme.
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5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop a
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