Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN: 9781305389892
Author: Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher: Cengage Learning
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Chapter 6, Problem 9TYK
Which of the following statements about inhibition is true?
a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme.
b. If an inhibitor binds the active site, it is considered noncompetitive.
c. If an inhibitor binds to a site other than the active site, this competitive inhibition.
d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable.
e. Competitive inhibition is usually not reversible.
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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.
A noncompetitive inhibition is best overcome (or reversed) by:
A. Increasing [enzyme]
B. Increasing [product]
C. Increasing [Substrate]
D. All of the above
A noncompetitive inhibitor (Circle one). a. Binds at the active site of the enzyme. b. Alters the three-dimensional structure of the enzyme. c. Increases the rate of the enzyme-catalyzed reaction. d. Has a structure similar to the substrate. e. Has its effect reversed by adding more substrate.
Chapter 6 Solutions
Biology: The Dynamic Science (MindTap Course List)
Ch. 6.1 - Prob. 1SBCh. 6.1 - In thermodynamics, what is meant by an isolated...Ch. 6.2 - Prob. 1SBCh. 6.2 - Prob. 2SBCh. 6.2 - Distinguish between exergonic and endergonic...Ch. 6.3 - Prob. 1SBCh. 6.3 - How are coupled reactions important to cell...Ch. 6.4 - How do enzymes increase the rates of the reaction...Ch. 6.4 - Can enzymes alter the G of a reaction?Ch. 6.5 - Prob. 1SB
Ch. 6.5 - What is the difference between competitive and...Ch. 6.5 - Prob. 3SBCh. 6.6 - Prob. 1SBCh. 6 - The capacity to do work best defines: a metabolic...Ch. 6 - The assembly of proteins from amino acids is best...Ch. 6 - When two glucose molecules react to form maltose:...Ch. 6 - When glucose reacts with ATP to form...Ch. 6 - In the following graph: A represents the product....Ch. 6 - Which of the following methods is not used by...Ch. 6 - In an enzymatic reaction: a. the enzyme leaves the...Ch. 6 - Which of the following statements about the...Ch. 6 - Which of the following statements about inhibition...Ch. 6 - Which of the following statements is incorrect? a....Ch. 6 - Prob. 11TYKCh. 6 - Discuss Concepts Trace the flow of energy through...Ch. 6 - Prob. 13TYKCh. 6 - Prob. 14TYKCh. 6 - Prob. 15TYKCh. 6 - Prob. 16TYKCh. 6 - Prob. 17TYKCh. 6 - Prob. 1ITDCh. 6 - Prob. 2ITDCh. 6 - Prob. 3ITD
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- Many pharmaceuticals exert their action by inhibiting the activity of enzymes. Choose the false statement regarding enzyme inhibition. A- Enzyme can be inhibited by a ligand that binds to an active site B- Enzyme can be inhibited by a ligand that binds to a site other than that of substrate C- Enzyme can be inhibited by a ligand that forms a covalent bond with enzyme. D- It is true of all enzyme inhibitors, that the degree of inhibition is reduced when the concentration of inhibitor is lowered by metabolism or E- Enzyme may be inhibited by a ligand that does not bind in the substrate sitearrow_forwardWhich of the folowing types of inhibitors binds to the active site of an enzyme? Select one: a. Competitive b. All of them C. Uncompetitive O d. Noncompetitivearrow_forwardA medicinal chemist is trying to determine the mechanism of action of inhibitors she has synthesized. The relative change in KM and Vmax upon incubation of the targeted enzyme with each inhibitor is shown in the table below. Inhibitor A Inhibitor B Inhibitor C Using this data, the mechanism of action of Inhibitor C is: Uncompetitive TS‡ analog Mixed Inhibition Competitive Кмарр- Км 0 Non-competitive app - Vmax <0 <0 0 Vmaxarrow_forward
- Which of the following statements about allosteric enzyme regulations are true. A. Allosteric regulations is always used to negatively regulate enzyme activity. B. Allosteric regulations are often end products of a biochemical pathway. C. Diffrent allosteric regulators turn enzyme activity on or off by binding the same site. D. Binding of allosteric regulators alters the conformation of an enzyme. B only B and C B and D D only A and Darrow_forwardA new drug has been discovered which inhibits the reaction catalyzed by enzyme A. The information on this drug is shown in the graph below. Based on this information, which one of the following is most correct about this drug? 1/No 2- inhibitor (0.1 uM] no inhibitor 11 1/[S), uM OA. competitive inhibitor binding to the substrate O B. competitive inhibitor binding to free enzyme A OC. uncompetitive inhibitor binding to [ES] O D. uncompetitive inhibitor binding to the Michaelis complex O E. allosteric enzymearrow_forwardAn allosteric inhibitor does which of the following? a. Binds to an enzyme away from the active site and changes the conformation of the active site, increasing its affinity for substrate binding. b. Binds to the active site and blocks it from binding substrate. c. Binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate. d. Binds directly to the active site and mimics the substrate.arrow_forward
- A. Which enzyme model involves the enzyme staying the same shape when the substrate binds to it? (lock and key, induced fit) B. If an inhibitor has similiar structure to that of a substrate, does it act as a competitive or noncompetitive inhibitor? C. What is the surface for an active site for an ezyme that binds the substrate to that site?arrow_forwardWhich of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.arrow_forwardWhat type of inhibition is occurring when the end product stops the action of the first enzyme in the video on feedback inhibition found below: https://www.youtube.com/watch?v=qHb7iieM2Ro Select one: a. competitive b. non-competitive c. Both competitive and non-competitive inhibition are illustrated in this video/figurearrow_forward
- In pure noncompetitive inhibition: a. Where on the enzyme does the inhibitor bind? b. Does the inhibitor bind to E, ES or both? c. What is the effect of I on Vmax? d. What is the effect of I on Km?arrow_forwardWhich 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.arrow_forwardWhich of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pHarrow_forward
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