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

An allosteric (non-competitive) inhibitor does which of the following?

Increases the affinity of the enzyme for its substrate, lowering the $K_m$.

Binds to a site other than the active site and decreases the maximum velocity ($V_{max}$) of the enzyme-catalyzed reaction.

Binds irreversibly to the enzyme, permanently inactivating it.

Competes with the substrate for binding at the active site, increasing the apparent $K_m$.

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Verified step by step guidance

Step 1: Begin by understanding the concept of allosteric inhibition. Allosteric inhibitors bind to a site on the enzyme that is distinct from the active site, which is why they are referred to as non-competitive inhibitors. This binding alters the enzyme's conformation and affects its activity.

Step 2: Recall the effect of allosteric inhibitors on enzyme kinetics. Unlike competitive inhibitors, allosteric inhibitors do not compete with the substrate for the active site. Instead, they decrease the enzyme's maximum velocity ($V_{max}$) without affecting the substrate's binding affinity ($K_m$).

Step 3: Analyze the options provided in the problem. The first option mentions increasing the enzyme's affinity for its substrate and lowering $K_m$, which is incorrect for allosteric inhibitors. The second option correctly describes the mechanism of allosteric inhibition: binding to a site other than the active site and decreasing $V_{max}$.

Step 4: Evaluate the third option, which states that the inhibitor binds irreversibly to the enzyme, permanently inactivating it. While irreversible inhibitors exist, they are not classified as allosteric inhibitors. This option is incorrect in the context of the problem.

Step 5: Consider the fourth option, which describes competitive inhibition. Competitive inhibitors compete with the substrate for the active site, increasing the apparent $K_m$. This is not the mechanism of allosteric inhibitors, making this option incorrect.