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

A noncompetitive inhibitor decreases the rate of an enzymatic reaction by:

increasing the enzyme's affinity for the substrate

binding irreversibly to the substrate, preventing its conversion to product

competing with the substrate for the active site, thereby increasing the $K_m$

binding to an allosteric site and reducing the maximum velocity ($V_{max}$) of the enzyme

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Verified step by step guidance

Step 1: Understand the concept of noncompetitive inhibition. Noncompetitive inhibitors bind to an allosteric site on the enzyme, which is a site other than the active site. This binding changes the enzyme's conformation, reducing its ability to catalyze the reaction effectively.

Step 2: Recognize that noncompetitive inhibitors do not compete with the substrate for the active site. Instead, they affect the enzyme's overall functionality, which impacts the reaction rate.

Step 3: Recall that noncompetitive inhibition decreases the maximum velocity ($V_{max}$) of the enzymatic reaction. This is because the enzyme's ability to convert substrate to product is reduced, regardless of the substrate concentration.

Step 4: Note that the Michaelis constant ($K_m$), which reflects the enzyme's affinity for the substrate, remains unchanged in noncompetitive inhibition. This is because the inhibitor does not interfere with substrate binding at the active site.

Step 5: Summarize the key effect: noncompetitive inhibitors bind to an allosteric site, altering the enzyme's structure and reducing its catalytic efficiency, which lowers the $V_{max}$ without affecting the $K_m$.