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 type of enzyme inhibitor does not alter the $K_m/V_{max}$ ratio of an enzyme?

Uncompetitive inhibitor

Competitive inhibitor

Noncompetitive inhibitor

Allosteric inhibitor

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Verified step by step guidance

Understand the concept of enzyme kinetics: Enzyme inhibitors affect the activity of enzymes by interacting with them in various ways. The $K_m$ (Michaelis constant) and $V_{max}$ (maximum velocity) are key parameters in enzyme kinetics that describe the enzyme's efficiency and capacity.

Define the types of enzyme inhibitors: Competitive inhibitors bind to the active site of the enzyme, uncompetitive inhibitors bind only to the enzyme-substrate complex, noncompetitive inhibitors bind to a site other than the active site, and allosteric inhibitors regulate enzyme activity by binding to allosteric sites.

Analyze the effect of noncompetitive inhibitors: Noncompetitive inhibitors decrease the $V_{max}$ because they reduce the overall number of active enzyme molecules, but they do not affect the $K_m$ since the substrate binding affinity remains unchanged. This means the $K_m/V_{max}$ ratio remains constant.

Compare with other inhibitors: Competitive inhibitors increase the $K_m$ without affecting $V_{max}$, uncompetitive inhibitors decrease both $K_m$ and $V_{max}$ proportionally, and allosteric inhibitors can have varied effects depending on whether they are activators or inhibitors.

Conclude that noncompetitive inhibitors are the type of enzyme inhibitor that does not alter the $K_m/V_{max}$ ratio, as their mechanism of action specifically impacts $V_{max}$ without changing $K_m$.