Biology: Life on Earth with Physiology Plus Mastering Biology with Pearson eText -- Access Card Package (11th Edition)
11th Edition
ISBN: 9780133910605
Author: Gerald Audesirk, Teresa Audesirk, Bruce E. Byers
Publisher: PEARSON
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Chapter 6, Problem 5MC
Summary Introduction
Introduction:
Competitive inhibition is a process in which the inhibitor binds to the active site of the enzyme and blocks the formation of the product from the substrate. The examples include sarin chemical and insecticide such as malathion inhibits the active site of the enzyme acetylcholinesterase. Many drugs like aspirin, penicillin, and ibuprofen act as a competitive inhibitor of the enzymes in the human body. Allosteric regulation involves the binding of the inhibitor on some other pocket rather than the binding site itself.
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Students have asked these similar questions
Sulfa drugs can be effective in limiting bacterial infections in humans while not producing toxic effects within human cells. Sulfa drugs most likely as as which of the following?
a. noncompetitive inhibitor of an enzyme required by bacteria but not human cells
b. allosteric effector increasing catalytic action of a bacterial enzyme
c. positive allosteric effector of an enzyme in bacterial cell wall synthesis
d. competitive inhibitor of an enzyme required by bacteria but not human cells
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 D
CTP is a known inhibitor of ATCase, the enzyme that catalyzes the first reaction in the pathway for the synthesis of this compound. This is an example of
a.
irreversible inhibition
b.
negative cooperativity
c.
protease inhibition
d.
feedback inhibition
Chapter 6 Solutions
Biology: Life on Earth with Physiology Plus Mastering Biology with Pearson eText -- Access Card Package (11th Edition)
Ch. 6.1 - Energy Unleashed Much like a cars engine, the...Ch. 6.1 - What other changes would help reduce fossil fuel...Ch. 6.1 - define energy and work?Ch. 6.1 - Could one design a roller coaster that didnt use...Ch. 6.1 - define potential energy and kinetic energy and...Ch. 6.1 - State and explain the first and second laws of...Ch. 6.2 - Energy Unleashed Marathoners rely on glycogen...Ch. 6.2 - describe how energy is captured and released by...Ch. 6.2 - Is glucose breakdown endergonic or exergonic? What...Ch. 6.2 - explain exergonic and endergonic reactions and...
Ch. 6.2 - explain activation energy?Ch. 6.3 - name and describe two important energy-carrier...Ch. 6.3 - Prob. 1TCCh. 6.3 - explain coupled reactions?Ch. 6.4 - explain how catalysts reduce activation energy?Ch. 6.4 - You may have seen the almost magical glow of...Ch. 6.4 - Can an enzyme catalyst make an endergonic reaction...Ch. 6.4 - explain how enzymes function as biological...Ch. 6.5 - describe how cells regulate the rate at which...Ch. 6.5 - Health Watch Lack of an Enzyme Leads to Lactose...Ch. 6.5 - Prob. 1TCCh. 6.5 - explain how poisons, drugs, and environmental...Ch. 6 - While vacuuming, you show off by telling a friend...Ch. 6 - Prob. 1FIBCh. 6 - Which of the following is True? a. Enzymes...Ch. 6 - Prob. 1RQCh. 6 - Refute the following: According to evolutionary...Ch. 6 - Prob. 2FIBCh. 6 - Prob. 2MCCh. 6 - Prob. 2RQCh. 6 - Can a bear use all the energy contained in the...Ch. 6 - Prob. 3FIBCh. 6 - Prob. 3MCCh. 6 - Prob. 3RQCh. 6 - Prob. 4FIBCh. 6 - Prob. 4MCCh. 6 - Prob. 4RQCh. 6 - Prob. 5FIBCh. 6 - Prob. 5MCCh. 6 - Prob. 5RQCh. 6 - Prob. 6FIBCh. 6 - Prob. 6RQCh. 6 - Prob. 7RQ
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- Which statement is/are TRUE about inhibitors? A. Mode of action of penicillin on bacteria is an example of irreversible inhibition. B. Increasing the substrate concentration does not affect competitive inhibitors C. Uncompetitive inhibitors bind only to the enzyme-substrate complex D. In the Lineweaver-Burke plot, the lines for enzymes in the presence and absence of noncompetitive inhibitor have different x-intercepts.arrow_forwardWhat are allosteric modulators? A. These are inhibitors that bind at sites other than the active site of enzymes resulting in the reduction of enzyme activities B. These are activators that bind at sites other than the active sites of enzymes resulting in enhanced enzyme activities. C. These are either inhibitors or activators that bind at the active site of enzymes. D. These are either inhibitors or activators that bind at sites other than the active sites of enzymes reducing or enhancing the latter's activities. E. These are small molecules that bind to an ES complex only.arrow_forwardWhich of the following statements about enzyme regulation is NOT true? a. covalent modification is one type of enzyme regulation. b. biologically most important type of regulation is standard inhibition. c. allosteric regulation can involved feedback inhibition. d. some types of enzume regulation are not widely used in biology. e. none of the abovearrow_forward
- Which 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_forwardWhich 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.arrow_forwardA3 Glucosylacetamide has a structure similar to the transition state during catalysis by the enzyme hexokinase and therefore would likely be A. covalently attached to hexokinase at a regulatory site distinct from the active site. B. covalently bound to an active site amino acid of hexokinase. C. a high-affinity hexokinase inhibitor. D. more rapidly hydrolyzed than ATP during catalysis.arrow_forward
- Which of the following is true about allosteric enzymes? A. Allosteric enzymes are always multimeric. B. Regulatory sites (allosteric sites) on an allosteric enzyme are always different from the catalytic site. C. Allosteric enzymes always change the conformation of the active site in response to binding of an allosteric modulator. D. Suicide inactivators are examples of allosteric modulators.arrow_forwardAn enzyme-substrate solution has been "poisoned" with a noncompetitive inhibitor. It is expected that the addition of more substrate to the solution will _____ the activity of the enzyme. a. increase b. decrease c. have no effect onarrow_forwardWhich of the following statements about the Michaelis Menten constant (Km) is correct......A. can be determined by plotting the data v/[S] against 1/[S] B. A large Km indicates a low affinity between the enzyme and the substrate C. A large Km means that a large concentration of substrate is needed for the enzyme to work D. is a measure of the affinity of enzymes for proteins, minerals and vitamins E. Small Km means that a large concentration of substrate is needed for the enzyme to workarrow_forward
- A noncompetitive inhibition is best overcome (or reversed) by: A. Increasing [enzyme] B. Increasing [product] C. Increasing [Substrate] D. All of the abovearrow_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_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_forward
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