8. Which of the following is characteristic of a competitive inhibitor of an enzyme-catalyzed reaction? A. The inhibitor binds covalently to the enzyme. B. The inhibitor increases the substrate binding affinity to the enzyme. C. In the presence of the inhibitor, the reaction exhibits an apparent increase in Km. D. In the presence of the inhibitor, the reaction exhibits an apparent decrease in Vmax- E. Increasing the substrate concentration fails to overcome the effects of the inhibitor.

8. Which of the following is characteristic of a competitive inhibitor of an enzyme-catalyzed reaction? A. The inhibitor binds covalently to the enzyme. B. The inhibitor increases the substrate binding affinity to the enzyme. C. In the presence of the inhibitor, the reaction exhibits an apparent increase in Km. D. In the presence of the inhibitor, the reaction exhibits an apparent decrease in Vmax- E. Increasing the substrate concentration fails to overcome the effects of the inhibitor.

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 6TYK: Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent...

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4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
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. Activatotrs are types of A. inhibitor B. cofactor C. enzyme D. substrate 2. Which of the following does NOT affect enzyme selectivity ? A. Electrostatic interactions B. Molecular shape C. hydrophillic Interactions D. None of these answers are correct
One of the hallmarks of competitive inhibition is that there is constant competition betweenthe substrate and the inhibitor for binding to the enzyme active site.a) If [inhibitor] >> [substrate], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?b) If [substrate] >> [inhibitor], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?
Which of the following statements about Competitive and noncompetitive inhibition is false? a. A noncompetitive inhibitor does not change the Km of the enzyme. b. A competitive inhibitor does not change the Vmax of the enzyme c. The noncompetitive inhibitor can bind either free enzyme or the enzyme–substrate complex. d.A competitive inhibitor decreases the apparent Km for a given substrate.
5. Which of the following statements is/are correct regarding allosteric regulation?a) Allosteric effector controls the activity of an enzyme by irreversible binding.b) Allosteric effector binds to the regulatory sitec) Allosteric activator causes changes in the catalytic site enhancing the substrate binding.d) Allosteric inhibitor causes changes in the catalytic site decreasing the substrate binding. explain each option
Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activation
In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.
1. When substrate concentration [S] << Km, the rate of an enzymatic reaction is increased by A. increasing kcat/Km B. increasing total enzyme concentration C. increasing [S] D. A and B E. A, B and C
The Vmax of an enzymatic reaction can be increased by _______________. A. Increasing the enzyme concentration only. B. Increasing the substrate concentration only. C. Removing a non-competitive inhibitor. D. Removing a competitive inhibitor. E. A and C F. A, C, and D
Drug D reversibly binds to enzyme E and inhibits its activity toward substrate S. D binds equally well whether or not S is bound. Sketch a graph of the expected 1/v vs. 1/[S] relationship for: A) The enzyme reacting with S in the absence of drug D, B) The enzyme reacting with S in the presence of a small amount of drug D, and C) The enzyme reacting with S in the presence of a large amount of drug D.
1. What is the relative activity and the degree of inhibition caused by a competitive