Microbiology: An Introduction
12th Edition
ISBN: 9780321929150
Author: Gerard J. Tortora, Berdell R. Funke, Christine L. Case
Publisher: PEARSON
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Textbook Question
Chapter 5, Problem 2R
DRAW ITUsing the diagrams below, show each of the following:
- a. where the substrate will bind
- b. where the competitive inhibitor will bind
- c. where the noncompetitive inhibitor will bind
- d. which of the four elements could be the inhibitor in feedback inhibition
- e. What effect will the reactions in (a), (b), and (c) have?
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Students have asked these similar questions
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
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.
What is the kinetical hallmark of reversible competitive inhibition?
A.
Vmax cannot be attained, even at high substrate concentrations.
B.
Vmax can be attained at sufficiently high concentrations of substrate.
C.
The apparent value for KM decreases as more inhibitor is added.
D.
The apparent value for KM remains unchanged as more inhibitor is added.
E.
Vmax decreases as more inhibitor is added.
Chapter 5 Solutions
Microbiology: An Introduction
Ch. 5 - Prob. 1RCh. 5 - DRAW ITUsing the diagrams below, show each of the...Ch. 5 - DRAW IT An enzyme and substrate are combined. The...Ch. 5 - Define oxidation-reduction, and differentiate the...Ch. 5 - There are three mechanisms for the phosphorylation...Ch. 5 - All of the energy-producing biochemical reactions...Ch. 5 - Fill in the following table with the carbon source...Ch. 5 - Write your own definition of the chemiosmotic...Ch. 5 - Why must NADH be reoxidized? How does this happen...Ch. 5 - NAME IT What nutritional type is a colorless...
Ch. 5 - Which substance in the following reaction is being...Ch. 5 - Which of the following reactions produces the most...Ch. 5 - Prob. 3MCQCh. 5 - Which of the following compounds has the greatest...Ch. 5 - Prob. 5MCQCh. 5 - Prob. 6MCQCh. 5 - Which culture produces the most lactic acid? Use...Ch. 5 - Which culture produces the most ATP? Use the...Ch. 5 - Which culture uses NAD+? Use the following choices...Ch. 5 - Which culture uses the most glucose? Use the...Ch. 5 - Explain why, even under ideal conditions,...Ch. 5 - The following graph shows the normal rate of...Ch. 5 - Compare and contrast carbohydrate catabolism and...Ch. 5 - How much ATP could be obtained from the complete...Ch. 5 - The chemoautotroph Acidithiobacillus can obtain...Ch. 5 - Haemophilus influenzae requires hemin (X factor)...Ch. 5 - The drug Hivid, also called ddC, inhibits DNA...Ch. 5 - The bacterial enzyme streptokinase is used to...
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- 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 abovearrow_forwardIn competitive inhibition, increasing concentrations of the inhibitor will have the following effect on the kinetics of the enzyme: A. Km will decrease. B. Vmax will stay the same. C. The reaction will cease because the inhibitor binds irreversibly. D. Km / Vmax will stay the same.arrow_forwardConcentration Effect : Substrate Concentration :: Inhibitor’s Effect : _____________________ A. Competitive Inhibition B. Noncompetitive Inhibition C. Enzyme Concentration D. Water Effects One factor affecting enzyme activity is the inhibitor's effect. How would you compare competitive inhibition from non-competitive inhibition? A. Non-competitive inhibition occurs when a molecule similar to the substrate binds to the active site, while competitive inhibition occurs when an inhibitor binds to the enzyme somewhere other than the active site. B. Competitive inhibition occurs when a molecule similar to the substrate binds to the active site, while non-competitive inhibition occurs when an inhibitor binds to the enzyme somewhere other than the active site.arrow_forward
- Inhibitor X exerts which of the following effects on the above enzyme (maltase)? (inhibitor X changes maltase activity to a Vo of 0.10 mM per minute when [S] = 0.125 mM, and a Vo of 0.25 mM per minute when [S] = 0.50 mM) competitive inhibition pure non-competitive inhibition uncompetitive inhibition all of the above none of the abovearrow_forwardThe Vmax of an enzymatic reaction can be increased by _______________. A. Increasing the enzyme concentration only. B. Increasing the substrate concentration only. C. Removing a non-competitive inhibitor. D. Removing a competitive inhibitor. E. A and C F. A, C, and Darrow_forwardWriteC if only statement A is correct, H if only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. A competitive inhibitor would bind at the enzyme's active site.B. As a result, the affinity of the substrate to the active site decreases.arrow_forward
- 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.arrow_forwardWhat 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 substratearrow_forwardA. Which enzyme model involves the enzyme staying the same shape when the substrate binds to it? (lock and key, induced fit) B. If an inhibitor has similiar structure to that of a substrate, does it act as a competitive or noncompetitive inhibitor? C. What is the surface for an active site for an ezyme that binds the substrate to that site?arrow_forward
- 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.arrow_forwardAn enzyme has 10 times greater affinity for substrate "A" than for substrate "B". Which of the following is true? a.) KM of A is 10 times the KM of B b.) The concentration of B is 10 times that of A c.) Vmax of A is 1/10 the Vmax of B d.) KM of A is 1/10 the KM of B e.) Vmax of A is 10 times the Vmax of Barrow_forwardA competitive inhibitor competes with substrate for binding to the active site of the enzyme. The enzyme, once bound by the inhibitor, is unable to form product. How would a competitive inhibitor affect the velocity of product formation? Would you need more or less of the substrate to get the same velocity as found before the inhibitor was added?arrow_forward
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