Biology - Study Guide
8th Edition
ISBN: 9780321501561
Author: Martha R. Taylor
Publisher: PEARSON EDUCATION (COLLEGE)
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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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The energetic equivalent of two molecules of ATP is used to activate an amino acid, yet only one molecule of ATP is used. Explain.
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
Biology - Study Guide
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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- Students conducting research observe the rate of an enzyme-catalyzed reaction under various conditions with a fixed amount of enzyme in each sample. When will increasing the substrate concentration likely result in the greatest increase in the reaction rate?arrow_forward(a) Give the substrate for each of the following enzymes: (i) urease (ii) fructose oxidase (b) What is the difference between competitive and noncompetitive inhibition? (c) In feedback control, what type of regulator slows down the catalytic activity of the reaction series? Why aren't intermediate products in a reaction sequence used in feedback control?arrow_forwardWhy is the enzyme-catalyzed introduction of carbon–carbon double bonds into fatty acids called an electron transport system?arrow_forward
- Many biosynthetic pathways are regulated by feedback control, where the product of a pathway turns off an enzyme that catalyzes an early step in the pathway. Usually, this control comes from an allosteric interaction. Of the types of reversible enzyme inhibition (Competitive inhibition, Noncompetitive inhibition, and Uncompetitive inhibition), what type is most likely to occur in a feedback control mechanism like this and why?arrow_forwardGive the two reasons why anabolic reactions in metabolism are not exactly the reverse of catabolic pathway.arrow_forwardDetermine the class of enzyme that is most likely to catalyze each of the following reactions, see bottom Figure 6D:arrow_forward
- Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis?arrow_forwardThe active site of an enzyme is usually a groove or pocket on the surface that A) binds allosteric regulators of the enzyme. B) is involved in the catalytic reaction of the enzyme. C) is inhibited by the presence of a coenzyme or a cofactor.arrow_forwardSuggest a reason why heating a solution containing an enzyme markedly decreases its activity. Why is the decrease of activity frequently much less when the solution contains high concentrations of the substrate?arrow_forward
- Explain why some of the molecules are positioned away from the diagonal in the graph given below. What kind of processes are involved in this phenomenon? Moreover, explain differences and similarities between H-ATPases and H-PPases.arrow_forwardName three weak forces by which the substrates bind in the active site of an enzyme.arrow_forwardWhen 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_forward
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