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

How does a competitive inhibitor slow enzyme catalysis?

It binds to the active site of the enzyme, preventing substrate binding.

It irreversibly modifies the enzyme's active site.

It binds to an allosteric site, changing the enzyme's conformation.

It increases the enzyme's affinity for the substrate.

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Verified step by step guidance

Understand the concept of competitive inhibition: A competitive inhibitor is a molecule that resembles the substrate and competes for binding to the enzyme's active site. This prevents the substrate from binding and slows down enzyme catalysis.

Analyze the mechanism: Competitive inhibitors bind reversibly to the active site of the enzyme. Since the active site is occupied by the inhibitor, the substrate cannot bind, and the enzyme cannot catalyze the reaction.

Compare competitive inhibition to other types of inhibition: Unlike allosteric inhibitors, which bind to a site other than the active site and change the enzyme's conformation, competitive inhibitors directly block the active site without altering the enzyme's structure.

Evaluate the effect on enzyme kinetics: Competitive inhibition increases the apparent Km (Michaelis constant) of the enzyme because a higher substrate concentration is required to overcome the inhibitor and achieve the same reaction rate. However, Vmax (maximum reaction velocity) remains unchanged because the inhibition can be overcome at high substrate concentrations.

Identify the correct answer: Based on the explanation, the correct answer is 'It binds to the active site of the enzyme, preventing substrate binding.' This aligns with the mechanism of competitive inhibition.