Textbook Question
How would the following changes affect enzyme activity for an enzyme whose optimal conditions are normal body temperature and physiological pH?
a. raising the temperature from 37 °C to 60 °C
Ch.10 Proteins Workers of the Cell
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696
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Table of contents
- Ch.4 Introduction to Organic Compounds75
- Ch.5 Chemical Reactions19
- Ch.6 Carbohydrates Life's Sweet Molecules62
- Ch.7 States of Matter and Their Attractive Forces8
- Ch.8 Solution Chemistry Sugar and Water Do Mix4
- Ch.10 Proteins Workers of the Cell89
- Ch.11 Nucleic Acids Big Molecules with a Big Role69
- Ch.12 Food as Fuel An Overview of Metabolism65
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696Not the one you use?Change textbook
Chapter 6, Problem 54c
Indicate whether each of the following describes a competitive or a noncompetitive inhibitor.
c. The inhibitor competes with the substrate for the active site.
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Understand the two types of enzyme inhibitors: Competitive inhibitors bind to the active site of the enzyme, directly competing with the substrate. Noncompetitive inhibitors bind to a different site on the enzyme, altering its shape and function without directly competing for the active site.
Analyze the statement provided: 'The inhibitor competes with the substrate for the active site.'
Recognize that this description matches the behavior of a competitive inhibitor, as it directly competes with the substrate for access to the enzyme's active site.
Recall that in competitive inhibition, increasing the concentration of the substrate can overcome the effect of the inhibitor, as the substrate and inhibitor vie for the same binding location.
Conclude that the correct classification for this description is a competitive inhibitor, based on the defining characteristic of competition for the active site.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Competitive Inhibition
Competitive inhibition occurs when an inhibitor molecule competes with the substrate for binding to the enzyme's active site. This type of inhibition can be overcome by increasing the concentration of the substrate, as more substrate molecules can outcompete the inhibitor for the active site. The presence of a competitive inhibitor increases the apparent Km (Michaelis constant) of the enzyme but does not affect the maximum reaction velocity (Vmax).
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Enzyme Inhibition Concept 1
Active Site
The active site of an enzyme is a specific region where substrate molecules bind and undergo a chemical reaction. It is typically a pocket or groove on the enzyme's surface, formed by the unique three-dimensional structure of the enzyme. The shape and chemical environment of the active site are crucial for the enzyme's specificity and catalytic activity, allowing it to recognize and interact with particular substrates.
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Noncompetitive Inhibition
Noncompetitive inhibition occurs when an inhibitor binds to an enzyme at a site other than the active site, altering the enzyme's function regardless of whether the substrate is present. This type of inhibition decreases the overall number of active enzyme molecules available for catalysis, leading to a decrease in Vmax, while the Km remains unchanged. Noncompetitive inhibitors can bind to both the enzyme and the enzyme-substrate complex, making their effect independent of substrate concentration.
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Related Practice
Textbook Question
The enzyme urease functions in the body to catalyze the formation of ammonia and carbon dioxide from urea as shown:
Describe what effect the following changes would have on the rate of this reaction assuming a steady state has been reached:
a. adding excess urea
Textbook Question
Indicate whether each of the following describes a competitive or a noncompetitive inhibitor.
a. The structure of the inhibitor is similar to that of the substrate.
Textbook Question
Indicate whether each of the following describes a competitive or a noncompetitive inhibitor.
e. Adding more substrate to the reaction restores the enzyme activity.
Textbook Question
Give the name and three-letter abbreviation for the amino acid described by each of the following:
a. the nonpolar amino acid with a sulfur atom in its side chain
Textbook Question
Give the name and three-letter abbreviation for the amino acid described by each of the following:
a. the polar amino acid with a benzene ring in its side chain