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
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Textbook Question
Chapter 8, Problem 6IQ
In the following graph of an exergonic reaction with and without an enzyme catalyst, label parts a through e.
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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
Michaelis–Menten kinetics
Lineweaver–Burk plot
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.
The following table provides descriptions of what is occurring at steps A, B, and C in the reaction. Review the descriptions and then choose the letter from the image that matches each description in the left-hand column of the table.
Which of the following statements are true for BOTH the "transition state" and an
"intermediate" of reaction? (This is a multi-select question, select all that apply.).
Both are only observed in enzyme-catalyzed reactions.
Both can be converted to product(s) or might decompose back to the reactant(s).
Neither are part of the "net equation" for the reaction.
Both contain covalent bonds are in the process of breaking and/or forming.
Both are part of every chemical reaction. (i.e. the mechanisms of all chemical
reactions, whether enzyme catalyzed or not, will have involve both a transition
state and an intermediate).
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
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- Given the following reactions, identify the class and subclass of the enzyme involvedarrow_forwardAn 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_forwardConsider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pesarrow_forward
- Consider a reaction in which reactants X and Y combine to form the product Z. The diagram below compares the reaction coordinates for the catalyzed and uncatalyzed pathways of this reaction. B. X+Y Reaction Coordinate What does letter B represent? O Letter B represents the activation energy of the uncatalyzed reaction pathway. Letter B represents the energy difference between the reactants and products for the uncatalyzed pathway. O Letter B represents the activation energy of the catalyzed reaction pathway. Letter B represents the energy difference between the reactants and products for the catalyzed pathway. Energyarrow_forwardConsider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction O c. The enzyme stabilizes the transition state for the reaction Od. The reaction is exergonic е. The reaction is now spontaneous due to the addition of enzyme Released Energyarrow_forwardGiven the following enzyme-catalyzed reaction, identify the class and subclass of the enzyme involved. HO Class: [Select] COO™ NH3* Subclass: [Select] H₂O H₂C= COO™ NH3*arrow_forward
- When calculating the order of a reaction, the enzyme doesnot appear in the equation. Explain.arrow_forwardMost of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: Give the Michaelis-Menten equation of an enzyme reaction and draw the Michaelis-Menten plot of [S] versus V0.arrow_forwardBelow is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the catalytic efficiency for this reaction. Report your answer in scientific notation to three significant figures in units of M-1s-1.arrow_forward
- Given the following enzyme catalyzed reaction, identify the class and subclass of the enzyme involved: NADH NAD* + H* C-O C-OT C=0 H-C-OH CH CH Class: Subclass:arrow_forwardGive a complete and well descriptive definition of the following:1.1 Enzyme catalysis1.2 Co-enzyme1.3 Negative heterotropic co-cooperativitarrow_forwardShow the complete reaction mechanism (including arrow pushing) for this reaction.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License