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 these statements about enzyme inhibitors is true?

Uncompetitive inhibitors bind only to the free enzyme, not the enzyme-substrate complex.

Noncompetitive inhibitors decrease the $K_m$ of the enzyme.

Competitive inhibitors increase the apparent $K_m$ but do not affect $V_{max}$.

Competitive inhibitors bind to an allosteric site on the enzyme.

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Verified step by step guidance

Step 1: Begin by understanding the types of enzyme inhibitors mentioned in the problem: competitive, uncompetitive, and noncompetitive inhibitors. Each type affects enzyme kinetics differently.

Step 2: Recall that competitive inhibitors bind to the active site of the enzyme, competing with the substrate. This increases the apparent $K_m$ (Michaelis constant) because a higher substrate concentration is needed to achieve the same reaction rate. However, $V_{max}$ (maximum reaction velocity) remains unchanged because the inhibitor can be overcome by increasing substrate concentration.

Step 3: Uncompetitive inhibitors bind only to the enzyme-substrate complex, not the free enzyme. This decreases both $K_m$ and $V_{max$, as the inhibitor stabilizes the enzyme-substrate complex and prevents product formation.

Step 4: Noncompetitive inhibitors bind to an allosteric site on the enzyme, not the active site. They decrease $V_{max}$ because they affect the enzyme's ability to catalyze the reaction, but they do not change $K_m$ since substrate binding is unaffected.

Step 5: Evaluate the statements provided in the problem. The correct answer is: 'Competitive inhibitors increase the apparent $K_m$ but do not affect $V_{max}$,' as this aligns with the known effects of competitive inhibition on enzyme kinetics.