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

Which of the following best explains the effect of a competitive inhibitor on enzyme-catalyzed reactions?

It increases both $K_m$ and $V_{max}$.

It decreases both $K_m$ and $V_{max}$.

It increases the apparent $K_m$ without affecting $V_{max}$.

It decreases $V_{max}$ without changing $K_m$.

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Verified step by step guidance

Understand the concept of competitive inhibition: A competitive inhibitor binds to the active site of the enzyme, competing directly with the substrate. This prevents the substrate from binding, but the inhibitor does not affect the enzyme's ability to catalyze the reaction once the substrate is bound.

Analyze the effect on $K_m$: Competitive inhibition increases the apparent $K_m$ because a higher substrate concentration is required to achieve the same reaction rate as in the absence of the inhibitor. This is due to the competition between the substrate and the inhibitor for the active site.

Analyze the effect on $V_{max}$: Competitive inhibitors do not affect $V_{max}$ because the enzyme can still reach its maximum reaction rate if a sufficiently high concentration of substrate is present to outcompete the inhibitor.

Compare the options provided: Evaluate each statement based on the effects of competitive inhibition. For example, the statement 'It increases both $K_m$ and $V_{max}$' is incorrect because $V_{max}$ remains unchanged.

Conclude with the correct explanation: The correct answer is 'It increases the apparent $K_m$ without affecting $V_{max}$,' as this aligns with the known effects of competitive inhibitors on enzyme kinetics.