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 of the following does NOT slow down or stop an enzyme’s rate of reaction?

Presence of a heavy metal ion that denatures the enzyme

Increasing substrate concentration (when enzyme is not saturated)

Competitive inhibitor binding to the active site

Noncompetitive inhibitor binding to an allosteric site

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Verified step by step guidance

Understand the factors that affect enzyme activity: Enzyme activity can be influenced by inhibitors, substrate concentration, and environmental conditions. Competitive inhibitors bind to the active site, noncompetitive inhibitors bind to allosteric sites, and heavy metals can denature enzymes.

Analyze the role of heavy metal ions: Heavy metal ions can denature enzymes by disrupting their structure, which stops the enzyme's activity. This is a factor that slows down or stops the enzyme's rate of reaction.

Examine competitive inhibitors: Competitive inhibitors compete with the substrate for binding to the enzyme's active site. This reduces the enzyme's ability to catalyze the reaction, thereby slowing down the rate of reaction.

Examine noncompetitive inhibitors: Noncompetitive inhibitors bind to an allosteric site, causing a conformational change in the enzyme that reduces its activity. This also slows down the enzyme's rate of reaction.

Consider the effect of increasing substrate concentration: When the enzyme is not saturated, increasing substrate concentration generally increases the rate of reaction because more substrate molecules are available to bind to the enzyme's active site. This does NOT slow down or stop the enzyme's rate of reaction.