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
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 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 enzyme
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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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
- In studying an enzyme, you measure activity as a function of substrate, and find that your enzyme follows standard Michaelis-Menten kinetics. In subsequent studies, as part of a drug screen you have isolated an inhibitor of the enzyme, that when present at 10 mM significantly inhibits enzymatic activity when substrate concentration is low. Briefly describe experiments and expected outcomes to differentiate whether this inhibitor is a competitive inhibitor or a mixed inhibitor.arrow_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_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_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
- Enzyme 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_forwardDescribe this image Substrate Substrate Inhibitor Enzyme A Enzyme B Inhibitor Structures The left picture shows allosteric inhibition, the right shows non-allosteric inhibition O The right picture shows allosteric inhibition, the left shows non-allosteric inhibition Both pictures show allosteric inhibition Both pictures show non-allosteric inhibitionarrow_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_forward
- WriteC 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_forwardA biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme Barrow_forwardA noncompetitive inhibition is best overcome (or reversed) by: A. Increasing [enzyme] B. Increasing [product] C. Increasing [Substrate] D. All of the abovearrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License