An 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.

An 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.

Concepts of Biology

1st Edition

ISBN:9781938168116

Author:Samantha Fowler, Rebecca Roush, James Wise

Publisher:Samantha Fowler, Rebecca Roush, James Wise

Chapter4: How Cells Obtain Energy

Section: Chapter Questions

Problem 5RQ: Which of the following is not true about enzymes? a. They are consumed by the reactions they...

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Which of the following statements about non-competitive inhibitors is true? A) They bind at the active site of the enzyme and block access to the substrate. B) They bind at a location away from the active site. C) They function by changing the shape of the enzyme's active site. D) B and C
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.
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.
Molecule X is expected to be a non-competitive inhibitor of an enzyme. If the inhibitor was tested at a saturating level of substrate the following would be observed: a. The inhibitor would decrease the Vmax b. The inhibitor would increase the Km c. The inhibitor would decrease the Km d. The inhibitor would increase the Vmax e. The inhibitor would not change the Vmax
What is true about a competitive inhibitor of an enzyme? You can choose more than one a. it binds the active site b. it binds an allosteric site c. it physically blocks the substrate d. it warps the active site e. it can be overcome with large amounts of substrate
What is it called when the final product of an enzymatic pathway acts as a modulator for the first enzyme in the pathway? a. isoenzyme activation b. relative specificity c. feed back inhibition d. competitive inhibition
How can a noncompetitive inhibitor affect enzymeactivity without binding to the active site?a. It binds to another location on the enzyme, altering the active site shape.b. It physically blocks the entrance to the active site.c. It alters the shape of the substrate, making it difficult for it to bind to theactive site.d. It degrades the substrate.
The image shows the rate of an enzyme reaction under conditions of no inhibition, competitive inhibition, and noncompetitive inhibition as reactions labeled uninhibited, A, and B. Which of the following best explains what has occurred in the enzyme reactions? Reaction B shows competitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows noncompetitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows competitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor. Reaction B shows noncompetitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor.
Enzymes have similar responses to both changes in temperature and pH. The effect of both is on the a. rate of movement of the substrate molecules. b. strength of the chemical bonds within the substrate. c. three-dimensional shape of the enzyme. d. rate of movement of the enzyme.
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.
Which of the following is not true about enzymes?a. They are consumed by the reactions they catalyze.b. They are usually made of amino acids.c. They lower the activation energy of chemical reactions.d. Each one is specific to the particular substrate(s) to which it binds.
Where does inhibitor binds on enzyme in mixed inhibition? A Allosteric site B Binds on substrate C At active site D Does not bind on enzyme