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

Recap of Reversible Inhibition

Biochemistry

7. Enzyme Inhibition and Regulation

Recap of Reversible Inhibition

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Multiple Choice

Below are kinetic data comparing aldehyde dehydrogenase activity in the absence and presence of Agent A. What type of inhibitor is Agent A?

Competitive inhibitor.

Noncompetitive inhibitor.

Uncompetitive inhibitor.

Irreversible inhibitor.

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Verified step by step guidance

Examine the provided kinetic data table, which shows the initial reaction velocities (V0) of aldehyde dehydrogenase both in the absence and presence of Agent A at various substrate concentrations ([Alcohol], mM).

Notice that in the presence of Agent A, the maximum velocity (Vmax) of the enzyme reaction does not reach the same level as in its absence, indicating a change in Vmax.

Observe that the initial velocities in the presence of Agent A are consistently lower than those without the agent, even as substrate concentration increases, suggesting that the inhibitor affects the enzyme regardless of substrate concentration.

Consider the characteristics of different types of enzyme inhibitors: Competitive inhibitors increase the apparent Km without affecting Vmax, noncompetitive inhibitors decrease Vmax without changing Km, and uncompetitive inhibitors decrease both Km and Vmax.

Based on the data, where Vmax is reduced but Km remains unchanged, conclude that Agent A is a noncompetitive inhibitor, as it decreases the maximum reaction rate without affecting the substrate's affinity for the enzyme.