Biology 2e
2nd Edition
ISBN: 9781947172517
Author: Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher: OpenStax
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Textbook Question
Chapter 6, Problem 14RQ
An allosteric inhibitor does which of the following?
- Binds to an enzyme away from the active site and changes the conformation of the active site, increasing its affinity for substrate binding
- Binds to the active site and blocks it from binding substrate
- Binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate
- Binds directly to the active site and mimics the substrate.
Expert Solution & Answer
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Which of the following is characteristic of competitive inhibitors?
the inhibitor could bind to the active site or to an allosteric site on the enzyme.
the enzyme will mistake the inhibitor for its substrate, so that the inhibitor will
end up covalently bound to the enzyme.
the inhibitor can bind only AFTER the substrate has bound (i.e. it binds only to
the ES complex).
the inhibitor can bind reversibly at the substrate-binding site (the active site).
the inhibitor will lower the characteristic Vmax of the enzyme.
Please select all of the following statements that are true.
Cofactors involve the use of vitamins to assist enzymes
Competitive inhibitors bind to the same active site as the substrate.
When the substrate binds to the enzyme the reaction rate increases.
Non-competitive inhibitors can act as both inhibitors and activators.
Determine whether the following statements describe a reversible competitive inhibitor, a reversible noncompetitive inhibitor, or an irreversible inhibitor.
Both the inhibitor and the substrate cannot bind to the enzyme at the same time.
The structure of the inhibitor is similar to that of the substrate.
The addition of more substrate can reverse the inhibitor effect
It forms a covalent bond with the active site.
Chapter 6 Solutions
Biology 2e
Ch. 6 - Figure 6.8 Look at each of the processes shown,...Ch. 6 - Figure 6.10 If no activation energy were required...Ch. 6 - Figure 6.14 The hydrolysis of one ATP molecule...Ch. 6 - Energy is stored long-term in the bonds of and...Ch. 6 - DNA replication involves unwinding two strands of...Ch. 6 - Consider a pendulum swinging. Which type(s) of...Ch. 6 - Which of the following comparisons or contrasts...Ch. 6 - Which of the following is the best way to judge...Ch. 6 - Which of the following is not an example of an...Ch. 6 - In each of the three systems, determine the state...
Ch. 6 - The energy released by the hydrolysis of ATP is...Ch. 6 - Which of the following molecules is likely to have...Ch. 6 - Which of the following is not true about enzymes...Ch. 6 - An allosteric inhibitor does which of the...Ch. 6 - Which of the following analogies best describes...Ch. 6 - Does physical exercise involve anabolic and/or...Ch. 6 - Name two different cellular functions that require...Ch. 6 - Explain in your own words the difference between a...Ch. 6 - Describe the position of the transition state on a...Ch. 6 - Imagine an elaborate ant farm with tunnels and...Ch. 6 - Energy transfers take place constantly in everyday...Ch. 6 - Do you think that the Ea for ATP hydrolysis is...Ch. 6 - With regard to enzymes, why are vitamins necessary...Ch. 6 - Explain in your own words how enzyme feedback...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Which of the following are characteristics of catabolic metabolic pathways? (Choose all correct answers). Overall oxidation of initial substrates so redox reactions involve use of NAD+ as oxidizing agent, converted to NADH. Large initial substrates are broken down to smaller final products. Overall reduction of intial substrates so redox reactions involve use of NADPH as reducing agent, converted to NADP+. The pathways are overall exergonic (negative delta G). Net production of ATP as a result of the pathway. Essentially irreversiblearrow_forwardWhich of the following statements regarding competitive enzyme inhibition is correct? O The substrate and the inhibitor compete for the active site on the enzyme. The substrate competes with an enzyme for binding to an inhibitor O The inhibition effect is always irreversible. The inhibitor binds to site other than the active site.arrow_forwardWhen the enzyme hexokinase binds to glucose and ATP it undergoes a conformational change. All of the following are true about this enzyme-substrate binding EXCEPT: The active site changes shape so that it binds more tightly to the substrates The substrates are optimally positioned for the reaction to occur The substrates become contorted or strained, which increases their reactivity The activation energy of the reaction increasesarrow_forward
- Mark any/all that apply to uncompetitive inhibition: Group of answer choices: None of these is correct. The inhibitor does not resemble the substrate. The inhibitor can bind to both enzyme alone AND enzyme that is bound by substrate. Inhibition can be overcome by the addition of more substrate. KM/Vmax are equal for both the inhibited and the uninhibited reaction.arrow_forwardCompetitive inhibitors bind to the active site of the enzyme. None of the answers listed are correct. bind with substrate molecules. change the shape of the enzyme by binding at the allosteric site. O act like the active site and take substrates away from the enzyme.arrow_forwardMark any/all that apply to uncompetitive inhibition: Group of answer choices -KM/Vmax are equal for both the inhibited and the uninhibited reaction. -The inhibitor does not resemble the substrate. -Inhibition can be overcome by the addition of more substrate. -The inhibitor can bind to both enzyme alone AND enzyme that is bound by substrate. -None of these is correct.arrow_forward
- An enzyme facilitate catalysis by formation of ester bond with an alcoholic substrate. Which amino acid residues can facilitate such mechanism of catalysis? Select the correct response: Cys and Met Lys and Arg Ser and Tyr Glu and Asparrow_forwardClassify the items as competitive or noncompetitive inhibitors for control of enzyme action. Bind to the allosteric site on the enzyme Not influenced by the concentration of substrate Resemble the substrate Do not resemble thhe substrate Bind to active site of the enzymearrow_forwardWhich of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active sitearrow_forward
- In noncompetitive inhibition, can both the substrate and the inhibitor bind at the same time? I know the inhibitor changes the enzyme's conformation so it would lower the product formation, but what if the substrate were to bind first, and then the inhibitor binded afterwards?arrow_forwardWhich of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are truearrow_forwardIdentify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.arrow_forward
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