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

Why does denaturation prevent an enzyme from being able to catalyze its reaction?

Denaturation removes all cofactors from the enzyme, making it inactive.

Denaturation alters the enzyme's three-dimensional structure, disrupting the active site so substrates can no longer bind properly.

Denaturation increases the enzyme's affinity for its substrate, causing the reaction to proceed too quickly.

Denaturation causes the enzyme to become more rigid, enhancing its catalytic activity.

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Verified step by step guidance

Understand the concept of enzyme denaturation: Denaturation refers to the process where an enzyme loses its native three-dimensional structure due to external factors such as heat, pH changes, or chemical agents. This structural change disrupts the enzyme's functionality.

Recognize the importance of the enzyme's active site: The active site is a specific region on the enzyme where the substrate binds and the catalytic reaction occurs. The shape and chemical properties of the active site are crucial for substrate binding and reaction specificity.

Analyze how denaturation affects the active site: When an enzyme is denatured, its three-dimensional structure is altered, including the active site. This structural disruption prevents the substrate from binding properly, thereby halting the enzyme's catalytic activity.

Clarify why cofactors are not the primary issue in this context: While cofactors are important for enzyme activity, denaturation primarily impacts the enzyme's structure rather than directly removing cofactors. The loss of structural integrity is the key reason for the enzyme's inactivity.

Conclude that denaturation does not enhance enzyme activity: Denaturation does not increase substrate affinity or make the enzyme more rigid. Instead, it disrupts the enzyme's ability to function by altering its structure and active site.