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 9IQ
Both ATP and ADP serve as regulators of enzyme activity. In catabolic pathways, which of these two molecules would you predict acts as an inhibitor? Explain.
Predict which of these molecules would act as an activator.
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Back in 1962, Gerhart and Pardee developed a model for the regulation of the activity of the ATCase
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include a sentence explaining the physiological significance of your model.
For a lot of enzymes that work on fatty acids, the rate determining step is the release of the product from the active site. This means that the activation energy for product release is much higher than the free energy of catalysis. What enthalpic or entropic contributions would make the activation energy for product release so high and explain?
Does an enzyme-mediated reaction need the same, more, or less activation energy than the same reaction occurring without the presence of the enzyme? Explain why.
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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- If you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the structure of the transition state right after the enzyme attacks the first substrate. Think hard about what we have covered, and visualize that transition state accurately:arrow_forwardMany organisms are able to live in extremely cold or hot temperatures, for example, the thermophilic bacteria that live in the hot springs of Yellowstone National Park. Draw a figure representing the predicted activity curve for enzymes in bacteria found in these habitats.arrow_forwardConsider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.arrow_forward
- When studying the mechanism of the enzymatic reaction, functional groups were found that ensure the connection of the enzyme molecule with the substrate and take a direct part in the act of catalysis. What are these areas of the enzyme formed by these groups called? What functional structures form them and why?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 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_forwardWhich type of enzyme (Table) catalyzes the following (given) reactions?arrow_forward
- The energetic equivalent of two molecules of ATP is used to activate an amino acid, yet only one molecule of ATP is used. Explain.arrow_forwardA reaction in an anabolic pathway is found to have a large negative Gibbs Free energy. How likely is it that this reaction is a regulatory step in the pathway? Explain your answer.arrow_forwardEnzymes are proteins that increase the rate of chemical reactions by lowering the energy activation required to facilitate the process. Explain the generalized and sequential enzyme mechanism of action (hint: from substrates to products).arrow_forward
- A certain metabolic pathway can be diagrammed as (see pic1), where A, B, C, and D are the intermediates, and X, Y, and Z are the enzymes that catalyze the reactions. The physiological free energy changes for the reactions are (see pic.2). Solve, (a) Which reaction is likely to be a major regulatory point for the pathway? (b) If your answer in Part a was in fact the case, in the presence of an inhibitor that blocks the activity of enzyme Z, would the concentrations of A, B, C, and D increase, decrease, or not be aff ected?arrow_forwardThe mechanism of chymotrypsin is used as a model for studying enzyme reaction mechanisms. Answer the following questions related to chymotrypsin: 1. List the 3 amino acids in the catalytic triad of chymotrypsin. 2. List the types of catalytic mechanisms (from the 3 main types of catalytic mechanisms) displayed in the mechanism of chymotrypsin.arrow_forwardWhen enzyme solutions are heated, there is a progessive loss of catalytic activty over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 degrees Celsius lost 50% of its activity in 12 minutes, but when incubated at 45 degrees Celsius in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates.arrow_forward
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