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

Under which of the following circumstances may the enzyme arginase in the liver change its shape and become inactive?

When an allosteric inhibitor binds to a site other than the active site

When substrate concentration is increased beyond saturation

When a competitive inhibitor binds to the active site

When the enzyme is exposed to optimal pH and temperature

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Verified step by step guidance

Understand the concept of enzyme inhibition: Enzymes can be regulated by inhibitors, which are molecules that decrease their activity. These inhibitors can be classified as competitive, non-competitive, or allosteric inhibitors.

Define allosteric inhibition: Allosteric inhibitors bind to a site other than the active site of the enzyme, causing a conformational change in the enzyme's structure. This change can render the enzyme inactive or reduce its activity.

Analyze the role of substrate concentration: When substrate concentration is increased beyond saturation, the enzyme's active sites are fully occupied, but this does not change the enzyme's shape or render it inactive. It simply means the enzyme is working at maximum capacity.

Examine competitive inhibition: Competitive inhibitors bind directly to the active site of the enzyme, preventing the substrate from binding. This does not change the enzyme's shape but temporarily blocks its activity.

Evaluate the effect of optimal pH and temperature: Enzymes function best at their optimal pH and temperature. Exposure to these conditions does not cause the enzyme to change shape or become inactive; instead, it enhances its activity.