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

6. Enzymes and Enzyme Kinetics

Enzyme Kinetics

Biochemistry

6. Enzymes and Enzyme Kinetics

Enzyme Kinetics

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Multiple Choice

Assuming the [S] is always saturating the enzymes (E), which of the plots below is correct?

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Understand the concept of enzyme kinetics: When substrate concentration [S] is saturating, the reaction rate (v) is directly proportional to the enzyme concentration [E]. This is because all enzyme active sites are occupied by the substrate, and the reaction rate depends on the amount of enzyme available.

Analyze the first plot: The reaction rate increases rapidly with enzyme concentration and then plateaus. This suggests that the reaction rate is initially dependent on enzyme concentration but becomes independent as it reaches a maximum rate (Vmax).

Analyze the second plot: The reaction rate decreases as enzyme concentration increases, which is not consistent with enzyme kinetics under saturating substrate conditions.

Analyze the third plot: The reaction rate initially increases and then decreases with increasing enzyme concentration. This is not typical for enzyme kinetics under saturating substrate conditions.

Analyze the fourth plot: The reaction rate increases linearly with enzyme concentration, which is consistent with the expectation that the reaction rate is directly proportional to enzyme concentration when substrate is saturating.