Microbiology: An Introduction, Global Edition
12th Edition
ISBN: 9781292099149
Author: Tortora J. Gerard
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
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.
Graph a double reciprocal plot that satisfy the following:
a. Michaelis-Menten kinetics enzyme,
b. an inhibitor that binds only free enzyme (competitive),
c. an inhibitor that binds only enzyme-substrate complex.
A medicinal chemist is trying to determine the mechanism of action of inhibitors she has
synthesized. The relative change in KM and Vmax upon incubation of the targeted enzyme with
each inhibitor is shown in the table below.
Inhibitor A
Inhibitor B
Inhibitor C
Using this data, the mechanism of action of Inhibitor C is:
Uncompetitive
TS‡ analog
Mixed Inhibition
Competitive
Кмарр- Км
0
Non-competitive
app - Vmax
<0
<0
0
Vmax
Chapter 5 Solutions
Microbiology: An Introduction, Global Edition
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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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
- A new drug has been discovered which inhibits the reaction catalyzed by enzyme A. The information on this drug is shown in the graph below. Based on this information, which one of the following is most correct about this drug? 1/No 2- inhibitor (0.1 uM] no inhibitor 11 1/[S), uM OA. competitive inhibitor binding to the substrate O B. competitive inhibitor binding to free enzyme A OC. uncompetitive inhibitor binding to [ES] O D. uncompetitive inhibitor binding to the Michaelis complex O E. allosteric enzymearrow_forwardPenícillin is an esxample of what type of enzyme inhíbitor? A. Competitive B. Noncompetitive C. Uncompetitive D. Irreveralble What type of Inhíbition ia observed from the ahift of the Lineweaver-Burke plot ahown in the graph below where the solid line represents the uninhibited enzymatic reaction while the broken line represents the inhibited enzymatic reaction? A. Irreveraible inhibition B. Noncompetitive inhibition C. Competitive inhíbition D. Uncompetitive inhibition Potaszium cyanide ia a polzon which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with reapect to reduced cytochrome c. Which type of inhíbition does this represent? 9. A. Irreveraible inhibition B. Noncompetitive inhibition C. Competitive inhibition D. Uncompetitive inhibition Which of the following enzyme clesses catalyze reactions in which two molecules become diasociated from each other? 10. A. Kinase В. Нydrolaae C. Isomerase D. Ligase 1. Which of the…arrow_forwardIn pure noncompetitive inhibition: a. Where on the enzyme does the inhibitor bind? b. Does the inhibitor bind to E, ES or both? c. What is the effect of I on Vmax? d. What is the effect of I on Km?arrow_forward
- A plot of 1/Vo versus 1/[S], called Lineweaver-Burk or double-reciprocal plot, is a useful tool for identifying the type of enzyme inhibition. What is the type of inhibition indicated by the graph? with inhibitor MS) OA Uncompetitive inhibition OB. Competitive inhibition The type of inhibition cannot be determined from the graph provided. OC. O D. Noncompetitive inhibtionarrow_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. An inhibitor that binds somewhere in the enzyme other than the active site is an uncompetitive inhibitor. B. With this mode of inhibitor binding, the substrate's affinity to the enzyme is affected and it decreases the maximum reaction velocity.arrow_forwardWhat type of inhibition is occurring when the end product stops the action of the first enzyme in the video on feedback inhibition found below: https://www.youtube.com/watch?v=qHb7iieM2Ro Select one: a. competitive b. non-competitive c. Both competitive and non-competitive inhibition are illustrated in this video/figurearrow_forward
- Write Cifonly statement A is correct, Hif only statement B is correct, Eif both statements are correct, Mif both statements are incorrect. A. When an inhibitor binds to the enzyme-substrate complex, the inhibition mode is uncompetitive. B. As a consequence, the enzyme's efficiency is decreased along with the maximum velocity.arrow_forwardOn the graph provided, sketch a plot of Vo/Vmax vs. [S] for an allosteric enzyme, 1.0 0.8 0.6 0.4 02 [Substrate] A. in the absence of any other ligand besides the substrate B. in the presence of an allosteric inhibitor C. in the presence of an allosteric activator. Clearly LABEL the 3 curves A, B and Carrow_forwardInhibitor 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_forward
- A. 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_forwardTo investigate the effects of a newly discovered inhibitor and enzymology list obtained the results showed in the figure below. Which statement best describes the binding of its inhibitor on the enzyme? ~y=0.768r+4.7425 3-0.568x+46576 19 . . . . ● x X The inhibitor binds at the active site. The inhibitor binds away from the active site, but after substrate binding. The inhibitor binds away from the active site before or after substrate binding. The inhibitor binds close to the active site, but after substrate binding. The inhibitor binds close to the active site, but prior to substrate binding. red by a strainarrow_forwardEnzyme X follows Michaelis-Menten kinetics. You add an inhibitor to your enzyme and you notice that the Vmax has decreased while the Km for enzyme X has increased as a result of adding the inhibitor. What are you able to conclude from this information? The inhibitor must be competitive The amount of total enzyme available to catalyze the reaction in the presence of the inhibitor has likely decreased The enzyme has a higher affinity for its substrate in the presence of the inhibitor The substrate concentration required to reach 1/2 of the maximum velocity for this enzyme has increased as a result of the inhibitor More than one of the above are conclusions that can be drawn from this informationarrow_forward
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