E. Indicate whether each of the following statements describes a: - reversible competitive inhibitor - reversible noncompetitive inhibitor -irreversible inhibitor An inhibitor that decreases enzyme activity by binding to a site on the enzyme other than the active site. An inhibitor that has a shape and charge distribution similar to that of the enzyme's normal substrate. The inhibitor and substrate can bind to the enzyme simultaneously An inhibitor that inactivates enzymes by forming a strong covalent bond at the enzyme active site. Both inhibitor and substrate bind at the active site on a random basis. The inhibitor effect cannot be reversed by the addition of more substrate. Inhibitor structure does not have to resemble substrate structure.

E. Indicate whether each of the following statements describes a: - reversible competitive inhibitor - reversible noncompetitive inhibitor -irreversible inhibitor An inhibitor that decreases enzyme activity by binding to a site on the enzyme other than the active site. An inhibitor that has a shape and charge distribution similar to that of the enzyme's normal substrate. The inhibitor and substrate can bind to the enzyme simultaneously An inhibitor that inactivates enzymes by forming a strong covalent bond at the enzyme active site. Both inhibitor and substrate bind at the active site on a random basis. The inhibitor effect cannot be reversed by the addition of more substrate. Inhibitor structure does not have to resemble substrate structure.

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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Indicate whether each of the following statements describes a reversible competitive inhibitor, a reversible noncompetitive inhibitor, or an irreversible inhibitor. More than one answer may apply.a. Both inhibitor and substrate bind at the active site on a random basis.b. The inhibitor effect cannot be reversed by the addition of more substrate.c. Inhibitor structure does not have to resemble substrate structure.d. The inhibitor and substrate can bind to the enzyme simultaneously
All of the following statements about competitive and non-competitive inhibitors are true EXCEPT:(a) Competitive inhibitors are structurally similar to anenzyme’s substrate and bind to the enzyme’s allostericsite.(b) Competitive inhibitors work by competing with a sub-strate for binding to an enzyme’s active site.(c) Noncompetitive inhibitors can bind at sites other thanthe active site of an enzyme, distorting the tertiary pro-tein structure, which alters the shape of the active site,rendering it ineffective for substrate binding.(d) Some noncompetitive inhibitors bind reversibly whilesome bind irreversibly to their enzyme.(e) b and d.
Classify 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 enzyme
Classify each specific inhibitor or inhibitor characteristic according to one of two types of inhibition: competitive or noncompetitive.
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.
An inhibitor was added to an enzyme and the expected rate of the reaction was not detected and the substrate was not utilized at all. This inhibitor is (choose one answer only): Is un-competitive, meaning the inhibitor binds to a site near the active site. Is competitive, meaning the inhibitor binds directly to the same active site as the subtrate. Is non-competitive, meaning the inhibitor binds to site other than the active site as the subtrate. Is irreversible, meaning the inhibitor binds covalently to the enzyme keeping the enzyme inactive permanently.
Explain the mode of action of enzymes in terms of an active site, enzyme and/or substrate complex, lowering of activation energy and enzyme specificity.
Mark 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.
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.
Explain the various forms of enzyme inhibitions in detail, using appropriate examples. Please be clear and concise.
Rank these substrates in order of best inhibitor (highest binding affinity) to worst inhibitor (lowest binding affinity). Rank from highest binding affinity to lowest binding affinity. To rank items as equivalent, overlap them.
Inhibitor X exerts which of the following effects on the above enzyme (lactase)? (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) pure non-competitive inhibition uncompetitive inhibition competitive inhibition all of the above none of the above