Campbell Biology (10th Edition)
10th Edition
ISBN: 9780321775658
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Chapter 8, Problem 4TYU
Summary Introduction
Introduction: Enzymes are macromolecules, which acts like the catalysts that increases the reaction without itself undergoing any change or without being consumed. Enzymes are the proteins.
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Why might an enzyme’s substrate, transition state, and product all serve as starting points for the design of a competitive inhibitor?
Why can we say that having a pure non- competitive inhibitor present is similar to just having less enzyme present?
Let's imagine I want to construct a competitive inhibitor for an enzyme one day. Should it be similar to the transition state, similar to the substrate, similar to the product, or form a covalent link with the enzyme?
Chapter 8 Solutions
Campbell Biology (10th Edition)
Ch. 8.1 - MAKE CONNECTIONS How does the second law of...Ch. 8.1 - Describe the forms of energy found in an apple as...Ch. 8.1 - WHAT IF? If you place a teaspoon of sugar in the...Ch. 8.2 - Cellular respiration uses glucose and oxygen,...Ch. 8.2 - VISUAL SKILLS How would the processes of...Ch. 8.2 - WHAT IF? Some nighttime partygoers wear glow-in-...Ch. 8.3 - How does ATP typically transfer energy from an...Ch. 8.3 - Prob. 2CCCh. 8.3 - MAKE CONNECTIONS Does Figure 8.11a show passive...Ch. 8.4 - Many spontaneous reactions occur very slowly. Why...
Ch. 8.4 - Prob. 2CCCh. 8.4 - WHAT IF? Malonate is an inhibitor of the enzyme...Ch. 8.4 - Prob. 4CCCh. 8.5 - How do an activator and an inhibitor have...Ch. 8.5 - Prob. 2CCCh. 8 - Explain how the highly ordered structure of a cell...Ch. 8 - Explain the meaning of each component in the...Ch. 8 - Describe the ATP cycle: How is ATP used and...Ch. 8 - How do both activation energy barriers and enzymes...Ch. 8 - Prob. 8.5CRCh. 8 - Choose the pair of terms that correctly completes...Ch. 8 - Prob. 2TYUCh. 8 - Which of the following metabolic processes can...Ch. 8 - Prob. 4TYUCh. 8 - Some bacteria art metabolically active in hot...Ch. 8 - If an enzyme is added to a solution where its...Ch. 8 - Prob. 7TYUCh. 8 - EVOLUTION CONNECTION Some people argue that...Ch. 8 - Prob. 9TYUCh. 8 - WRITE ABOUT A THEME: ENERGY AND MATTER Life...Ch. 8 - Prob. 11TYU
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- Why must you only add the enzyme after all the other reagents have been added? Because until all reagents have been added the reaction mixture will not have the correct pH and/or ionic strength which may result in the enzyme been denatured and/or having reduced activity. Because until all reagents have been added the reaction mixture will not be at the correct temperature which may result in the enzyme been denatured and/or having reduced activity. Because until all reagents have been added the reaction mixture will not have the correct amount of substrate which may result in the enzyme not working optimally. Because the enzyme needs to be kept cold as long as possible, so it is not denatured and/or having reduced activity.arrow_forwardWhy do we not determine the initial reaction rate when the enzyme is saturated with substrate?arrow_forwardIf an enzyme has a maximal activity of pH 6.8 and your reaction buffer is a pH 5.8, what do you need to do to increase the activity of the enzyme? add a dilute solution of sodium hydroxide to the reaction buffer to decrease the pH. add a dilute solution of sodium hydroxide to the reaction buffer to raise the pH. add a dilute solution of acid to the reaction buffer to raise the pH. add a dilute solution of acid to the reaction buffer to decrease the pH.arrow_forward
- Define the following terms enzyme kinetics competitive inhibition non-competitive inhibition allosteric inhibitionarrow_forwardCan same enzyme have different kinetics for different substrates? What is the biological significance that?arrow_forwardA competitive inhibitor competes with substrate for binding to the active site of the enzyme. The enzyme, once bound by the inhibitor, is unable to form product. How would a competitive inhibitor affect the velocity of product formation? Would you need more or less of the substrate to get the same velocity as found before the inhibitor was added?arrow_forward
- If the ATP-binding site of an enzyme is buried in the interior of the enzyme, in a hydrophobic environment, is the ionic interaction between enzyme and substrate stronger or weaker than that same interaction would be on the surface of the enzyme, exposed to water? Why?arrow_forwardFour important properties of enzymes are high catalytic rate,high degree of substrate specificity, negligible formation ofside products, and _____________________.arrow_forwardWhat would be the result of an enzyme having a greater binding energy for the substrate than for the transition state?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_forwardAn enzyme catalyzes the following reaction. Which of the following inhibitors would you expect to be competitive inhibitors and which non-competitive inhibitors? Please explain briefly.arrow_forwardWhat are enzymes? What distinguishes enzymes from regular chemical catalysts? On the specificity of enzyme action, please comment. Which factor accounts for their specificity the most? Describe the enzyme catalysis mechanism.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License