Prescott's Microbiology
10th Edition
ISBN: 9781259281594
Author: Joanne Willey, Linda Sherwood Adjunt Professor Lecturer, Christopher J. Woolverton Professor
Publisher: McGraw-Hill Education
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Textbook Question
Chapter 10.6, Problem 5RIA
What are competitive and noncompetitive inhibitors, and how do they inhibit enzymes?
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What is the difference between competitive and noncompetitive inhibitors?
Why are irreversible enzyme inhibitors referred to as poisons?
How can we tell whether a reversible inhibitor inhibits in a competitive, noncompetitive, or noncompetitive manner?
Chapter 10 Solutions
Prescott's Microbiology
Ch. 10.1 - Figure 10.2 The Relationship of G to the...Ch. 10.1 - What kinds of work are carried out in a cell?...Ch. 10.1 - What is thermodynamics? Summarize the first and...Ch. 10.1 - Define entropy and enthalpy. Do living cells...Ch. 10.1 - Prob. 4RIACh. 10.1 - Prob. 5RIACh. 10.2 - Why is ATP called a high-energy molecule? How is...Ch. 10.2 - Describe the energy cycle and ATPs role in it....Ch. 10.3 - Prob. 1MICh. 10.3 - Prob. 2MI
Ch. 10.4 - Figure 10.6 Electron Movement and Reduction...Ch. 10.4 - How is the direction of electron flow between...Ch. 10.4 - When electrons flow from the NAD+/NADH conjugate...Ch. 10.4 - Which among the following would be the best...Ch. 10.4 - In general terms, how is G related to E0? What is...Ch. 10.4 - Name and briefly describe the major electron...Ch. 10.6 - Will an enzyme with a relatively high Km have a...Ch. 10.6 - Prob. 2MICh. 10.6 - What is an apoenzyme? A holoenzyme? What are the...Ch. 10.6 - Illustrate the effect enzymes have on the...Ch. 10.6 - How does enzyme activity change with substrate...Ch. 10.6 - What special properties might an enzyme isolated...Ch. 10.6 - What are competitive and noncompetitive...Ch. 10.6 - How are enzymes and ribozymes similar? How do they...Ch. 10.7 - Figure 10.19 Allosteric Regulation. The structure...Ch. 10.7 - Figure 10.21 Feedback Inhibition. Feedback...Ch. 10.7 - Briefly describe the three ways a metabolic...Ch. 10.7 - Define the terms metabolic channeling and...Ch. 10.7 - Define allosteric enzyme and allosteric effector.Ch. 10.7 - Prob. 4RIACh. 10.7 - Prob. 5RIACh. 10.7 - What is the significance of the fact that...Ch. 10 - Examine the structures of macromolecules in...Ch. 10 - Most enzymes do not operate at their biochemical...Ch. 10 - Examine the branched pathway shown here for the...Ch. 10 - Prob. 4CHI
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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
- What are the four key types of irreversible inhibitors that can be used to study enzyme function?arrow_forwardHow can you distinguish between a competitive inhibitor and an uncompetitive inhibitor experimentally?arrow_forwardHow does competitive inhibition differ from non-competitive inhibition?arrow_forward
- What is enzyme catalysis? How it is affected by various chemical & Physical factors?arrow_forwardWhat are some differences and/or similarities in the type of inhibition caused by heat, acid or base, and heavy metal ions on enzyme activity?arrow_forwardWhat causes competitive inhibition?arrow_forward
- What is the difference between competitive and non-competitive inhibition? How can each be reversed?arrow_forward. Based on what you know about enzyme inhibition, classify the following examples as irreversible, competitive, or noncompetitive enzyme inhibition. A) competitive B) noncompetitive C) irreversible 1) Diisopropyl fluorophosphate binds to acetylcholinesterase and permanently inactivates the enzyme. Paralysis results. 2) A drug binds to the active site of an enzyme but disassociates and leaves the enzyme active. 3) A toxin binds to the surface of an enzyme. The enzyme then binds the substrate, but no product is produced. The toxin may disassociate and the enzyme will become active again. 4) Vitamin K is a coenzyme involved in blood clotting. An anticoagulant drug binds at the site of vitamin K bonding, blocking vitamin K binding and preventing clotting. Clotting resumes after the patient stops taking the drug. 5) Aspirin binds to prostaglandin synthetase and permanently stops its ability to produce prostaglandin.arrow_forwardWhat is the relative inhibition of an enzyme by a competitive inhibitor at [S] = KS and [I] = KI?arrow_forward
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