Microbiology: Principles and Explorations
9th Edition
ISBN: 9781118743164
Author: Jacquelyn G. Black, Laura J. Black
Publisher: WILEY
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Textbook Question
Chapter 5, Problem 9SQ
All of the following statements about competitive and noncompetitive inhibitors are true EXCEPT:
- (a) Competitive inhibitors are structurally similar to an enzyme’s substrate and bind to the enzyme’s allosteric site.
- (b) Competitive inhibitors work by competing with a substrate for binding to an enzyme’s active site.
- (c) Noncompetitive inhibitors can bind at sites other than the active site of an enzyme, distorting the tertiary protein structure, which alters the shape of the active site, rendering it ineffective for substrate binding.
- (d) Some noncompetitive inhibitors bind reversibly while some bind irreversibly to their enzyme.
- (e) b and d.
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A mixed inhibitor of an enzyme (sometimes called a mixed non-competitive inhibitor) can decrease the rate of a reaction by any of the following EXCEPT by:
a) binding to a site other than the active site of the enzyme.
b) binding to the active site of the enzyme, preventing substrate binding.
c) decreasing kcat.
d) Increasing KM.
Which model for enzyme-substrate chemical complementarity is described by the following:
Before substrate binding, some enzyme molecules have active sites complementary to substrates and other enzyme molecules have non-complementary active sites. Substrate molecules preferentially bind to the enzyme molecules with complementary active sites. Non-complementary enzyme molecules undergo a structural change to become complementary to maintain conformational equilibrium.
a) conformational selection
b) induced fit
c) lock and key...
b) Enzymes accelerate reactions by facilitating the formation of the transition state. Define transition
state and activation energy. For full credit, you need to present the actual graph (for an endergonic or
exergonic reaction - make sure to specify your choice) highlighting each term?
c) Explain how an irreversible inhibitor for an enzymatic reaction differs from reversible inhibitors.
Provide specific example of an irreversible inhibitor and its target enzyme
d) Determine the Vo as a function of Vmax when the substrate concentration is equal to 10 KM or 20
KM. What does this tell you about an enzyme ability to reach Vmax?
Chapter 5 Solutions
Microbiology: Principles and Explorations
Ch. 5 - How are photosynthesis and respiration related to...Ch. 5 - What is the main difference between...Ch. 5 - Distinguish between coenzyme and cofactor. How are...Ch. 5 - Prob. 2.2SCCh. 5 - Prob. 3.1SCCh. 5 - If four actual molecules of ATP are produced for...Ch. 5 - Prob. 3.3SCCh. 5 - Prob. 3.4SCCh. 5 - Prob. 4.1SCCh. 5 - What is returned to chlorophyll in cyclic...
Ch. 5 - What were probably the first kind of...Ch. 5 - What type of metabolism is characteristic of...Ch. 5 - Prob. 1CCSCh. 5 - Suppose that you had a culture known to contain...Ch. 5 - In what sequence might the different kinds of...Ch. 5 - Prob. 3CTQCh. 5 - Which of the following is not true about...Ch. 5 - Prob. 2SQCh. 5 - Prob. 3SQCh. 5 - Prob. 4SQCh. 5 - Prob. 5SQCh. 5 - Prob. 6SQCh. 5 - Prob. 7SQCh. 5 - Prob. 8SQCh. 5 - All of the following statements about competitive...Ch. 5 - Prob. 10SQCh. 5 - What is feedback inhibition? (a) When the end...Ch. 5 - Which of the following is true regarding the...Ch. 5 - Prob. 13SQCh. 5 - Prob. 14SQCh. 5 - During aerobic cell respiration most of the energy...Ch. 5 - The typical end products of complete aerobic cell...Ch. 5 - Prob. 17SQCh. 5 - The end products of photosynthesis in...Ch. 5 - Which of the following final electron acceptors is...Ch. 5 - Prob. 20SQCh. 5 - Prob. 21SQ
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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
- 13.) An unchanged apparent Km results from the action of an uncompetitive inhibitor because A) the presence of the inhibitor can shift the binding equilibrium toward the ES complex. B) the presence of the inhibitor can shift the binding equilibrium toward the E + S state. C) the presence of excess substrate shifts the binding equilibrium toward the ES complex. D) uncompetitive inhibitors do not alter the binding equilibrium between substrate and enzyme. E) Uncompetitive inhibitors always result in a lower apparent Km, not an unchanged apparent Km.arrow_forwardCan you help mearrow_forwardDrug D reversibly binds to enzyme E and inhibits its activity toward substrate S. D binds equally well whether or not S is bound. Sketch a graph of the expected 1/v vs. 1/[S] relationship for: A) The enzyme reacting with S in the absence of drug D, B) The enzyme reacting with S in the presence of a small amount of drug D, and C) The enzyme reacting with S in the presence of a large amount of drug D.arrow_forward
- 2arrow_forwardThe activity of an enzyme can be regulated by a: A) competitive inhibitor binding to the active site. B) competitive inhibitor binding to the ES complex. C) noncompetitive inhibitor binding to the ES complex. D) Only A and C are correct. E) Only A and B are correct.arrow_forwardThe text discusses three forms of enzyme inhibition: uncompetitive inhibition, competitive inhibition, and irreversible inhibition.(a) Describe how an enzyme inhibitor of each type works.(b) What kinds of bonds are formed between an enzymeand each of these three kinds of inhibitors?arrow_forward
- A) Why most therapeutic inhibitors (prescription medications) that are enzyme inhibitors function through a competitive inhibition mechanism. B) Describe a circumstance/reason that a drug company would specifically choose to develop a medication that inhibited an enzyme through a mechanism other than competitive inhibition.arrow_forwardWhich of the following would best explain how an enzyme catalyzes two different reactions? A) The enzyme contains a-helices and B-pleated sheets. B) The enzyme is subject to cooperativity C) Either the enzyme has two distinct active sites or the substrates involved in the two reactions have very similar structures D) The enzyme is subject to competitive inhibition and allosteric regulation E) The enzyme is composed of at least two subunitsarrow_forward. Based on what you know about enzyme inhibition, classify the following examples as irreversible, competitive, or noncompetitive enzyme inhibition. A) competitive B) noncompetitive C) irreversible 1) Diisopropyl fluorophosphate binds to acetylcholinesterase and permanently inactivates the enzyme. Paralysis results. 2) A drug binds to the active site of an enzyme but disassociates and leaves the enzyme active. 3) A toxin binds to the surface of an enzyme. The enzyme then binds the substrate, but no product is produced. The toxin may disassociate and the enzyme will become active again. 4) Vitamin K is a coenzyme involved in blood clotting. An anticoagulant drug binds at the site of vitamin K bonding, blocking vitamin K binding and preventing clotting. Clotting resumes after the patient stops taking the drug. 5) Aspirin binds to prostaglandin synthetase and permanently stops its ability to produce prostaglandin.arrow_forward
- One of the hallmarks of competitive inhibition is that there is constant competition betweenthe substrate and the inhibitor for binding to the enzyme active site.a) If [inhibitor] >> [substrate], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?b) If [substrate] >> [inhibitor], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?arrow_forwardExplain how the following changes affect the rate of an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor: (a) increasing the substrate concentration at a constant inhibitor concentration, (b) decreasing the inhibitor concentration at a constant substrate concentration.arrow_forwardWhich of the following statements about isozymes is correct? (Select all that apply.) (a) Isozymes allow reactions to be optimized under different conditions. (b) The main reason for isozymes is so that a given reaction is never completely inhibited. (c) Isozymes have completely different active sites. (d) Bind the same substrates but form different products. (e) Isozymes display different physical properties, such as kinetic parameters.arrow_forward
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