Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 8, Problem 8IQ
Return to the diagram in Interactive Question 3.7, Draw a competitive inhibitor and a noncompetitive inhibitor and indicate where each would bind to the enzyme molecule.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Using enzyme kinetics, illustrate the cooperative behavior of allosteric enzymes (plot of reaction velocity versus substrate concentration for instance)
Please handraw this graph with all the necessary detailed information:
Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated with:
1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site.
2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.
Chapter 8 Solutions
Study Guide for Campbell Biology
Ch. 8 - Complete the following concept map that summarizes...Ch. 8 - Complete the following table to indicate how the...Ch. 8 - Develop a concept map on free energy and G. The...Ch. 8 - Prob. 4IQCh. 8 - Prob. 5IQCh. 8 - In the following graph of an exergonic reaction...Ch. 8 - In the following diagram of a catalytic cycle,...Ch. 8 - Return to the diagram in Interactive Question 3.7,...Ch. 8 - Both ATP and ADP serve as regulators of enzyme...Ch. 8 - What is the relationship between the concept of...
Ch. 8 - What role do enzymes play in metabolism?Ch. 8 - ________ the totality of an organisms chemical...Ch. 8 - _______ pathways that use energy to synthesize...Ch. 8 - Prob. 3TYKFCh. 8 - _______ the most random form of energyCh. 8 - _______ term for the measure of disorder or...Ch. 8 - Prob. 6TYKFCh. 8 - _______ inhibitors that decrease an enzymes...Ch. 8 - Prob. 8TYKFCh. 8 - Prob. 9TYKFCh. 8 - Prob. 10TYKFCh. 8 - Catabolic and anabolic pathways are often coupled...Ch. 8 - Which statement most closely reflects the first...Ch. 8 - When a cell breaks down glucose, only about 34% of...Ch. 8 - Prob. 4TYKCh. 8 - Prob. 5TYKCh. 8 - Prob. 6TYKCh. 8 - One way in which a cell maintains metabolic...Ch. 8 - Prob. 8TYKCh. 8 - Prob. 9TYKCh. 8 - What is meant by an induced fit? a. The binding of...Ch. 8 - In an experiment, changing the pH from 7 to 6...Ch. 8 - Prob. 12TYKCh. 8 - Penicillin binds to the active site of an enzyme...Ch. 8 - Prob. 14TYKCh. 8 - Prob. 15TYKCh. 8 - Which line in the diagram indicates the G of the...Ch. 8 - Prob. 17TYKCh. 8 - Prob. 18TYKCh. 8 - Prob. 19TYKCh. 8 - Prob. 20TYK
Knowledge Booster
Learn more about
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 purely competitive inhibitor of an enzyme has which of the following kinetic effects? decrease in Km increase in Vmax decrease in Vmax increase in Km Question 60 The Michaelis-Menten constant (KM) has the following characteristics, EXCEPT: The dimension for KM is concentration, such as molarity It is equal to ½ of Vmax It is the substrate concentration necessary to reach ½ of Vmaxarrow_forwardDifferentiate the concerted model and sequential model by illustrating the difference in terms of R and T forms of the enzyme when a substrate is about to bind. Write a shortdescription for each.arrow_forwardGraph 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.arrow_forward
- One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The turnover number for an enzyme (per second) is 752 How many molecules of substrate can one molecule of the enzyme act on in 19.2 min?arrow_forwardIn the scheme below which represents the mechanism of action for a large number of enzymes: A+B⟺AB⟶C The steady state approximation is reached when: d[AB]/dt≈0 k2≫k1 k−1≫k1 k−1=k1arrow_forwardGraph B above depicts Lineweaver-Burk double reciprocal plot for an enzyme catalyzed reaction carried out in the presence or absence of an inhibitor. Which of the following statement best describes the kinetic data shown below: ? Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor.arrow_forward
- Rearrange the following terms to show the process of enzymatic reaction. Use and + to complete the equation. enzyme enzyme-substrate complex enzyme product substrate Several important things should be noted about this reaction: 1. A/an because of the fit between their structures; 2. As a result, something happens to the example, it might be split in two at a particular location. 3. Then the and 4. The enzyme is again. 5. Note that the arrows in the formula for enzyme reaction point acts on a specific to form a/an molecule. For comes apart, yielding the in the reaction and is now free to react _- This means that the reaction is 6. An enzyme-substrate complex can simply go back to the the 7. The products of an enzymatic reaction can react with the enzyme to form the and again; 8. It, in turn, may again form the 9. Therefore, the same. and the may act to cause a to go either way.arrow_forwardusing the method for experiment below and the table conduct 1 graph of the different factors vs rate of enzyme activity. The experiment began by preparing a hot water bath by boiling water and an ice water bath using ice in a 400 mL beaker. In the control group, 2 mL of 3% H2O2 was placed in a test tube and a pinch of MnO2 was added. The rate of this reaction was assigned as 5, and the production of bubbles in millimeters (mm) was noted. The reaction was considered complete when no more bubbles were produced. Another control group was set up by placing 2 mL of 3% H2O2 in a test tube and adding a pinch of sand, with the rate of reaction assigned as 0. To investigate the difference between plant and animal catalase, 2 mL of H2O2 was added to a test tube and a small piece of fresh liver was added. The rate of reaction between 0-5 was noted, along with the production of bubbles in mm. The same procedure was repeated using a small piece of fresh potato. Next, the effect of…arrow_forwardThe molecule shown is an effective inhibitor of the enzyme hydrolase, explain how this likley occurs, use a diagram.arrow_forward
- An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.arrow_forwardThe figure displays the relationship between initial rate of product formation and reactant concentration in an enzyme-catalyzed reaction with a fixed amount of enzyme. Which of the following statements best explains the shape of the rate curve at high reactant concentration?arrow_forwardA 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 Vmaxarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSON
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
Anatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education
Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License