Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

7. Enzyme Inhibition and Regulation

Enzyme Inhibition

Biochemistry

7. Enzyme Inhibition and Regulation

Enzyme Inhibition

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Multiple Choice

A noncompetitive inhibitor decreases the rate of an enzyme reaction by _____.

binding to an allosteric site and reducing the maximum velocity ($V_{max}$) of the reaction

competing with the substrate for binding at the active site

increasing the affinity of the enzyme for its substrate

decreasing the substrate concentration

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Verified step by step guidance

Understand the concept of enzyme inhibition: Enzyme inhibitors are molecules that reduce the activity of enzymes. Noncompetitive inhibitors specifically bind to an allosteric site, which is a site other than the active site, and alter the enzyme's function.

Recognize the effect of noncompetitive inhibitors: Noncompetitive inhibitors do not compete with the substrate for the active site. Instead, they bind to the allosteric site and change the enzyme's shape or dynamics, reducing its ability to catalyze the reaction effectively.

Analyze the impact on reaction kinetics: Noncompetitive inhibition decreases the maximum velocity ($V_{max}$) of the reaction because the enzyme's efficiency is reduced. However, the substrate can still bind to the active site, so the affinity of the enzyme for the substrate (represented by $K_m$) remains unchanged.

Eliminate incorrect options: The option 'competing with the substrate for binding at the active site' describes competitive inhibition, not noncompetitive inhibition. The option 'increasing the affinity of the enzyme for its substrate' is incorrect because noncompetitive inhibitors do not affect substrate binding affinity. The option 'decreasing the substrate concentration' is unrelated to the mechanism of noncompetitive inhibition.

Conclude the correct answer: Noncompetitive inhibitors decrease the rate of an enzyme reaction by binding to an allosteric site and reducing the maximum velocity ($V_{max}$) of the reaction.