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

Michaelis-Menten Assumptions

Biochemistry

6. Enzymes and Enzyme Kinetics

Michaelis-Menten Assumptions

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Multiple Choice

Which of the following options is not an assumption made in deriving the Michaelis-Menten equation?

The value of k_-2 can be ignored.

The rate of ES formation = to rate of P formation.

The [E] is smaller than the [S].

a, b & c are all correct assumptions.

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Verified step by step guidance

Understand the Michaelis-Menten equation: It describes the rate of enzymatic reactions by relating reaction rate to substrate concentration, enzyme concentration, and two constants (Km and Vmax).

Identify the assumptions made in deriving the Michaelis-Menten equation: These include the steady-state assumption, where the formation and breakdown of the enzyme-substrate complex (ES) are balanced, and the assumption that the reverse reaction from product to substrate is negligible (k-2 is ignored).

Analyze the given options: The statement 'The rate of ES formation = to rate of P formation' is not a correct assumption. Instead, the rate of ES formation is equal to the rate of ES breakdown (to form product and revert to enzyme and substrate).

Consider the assumption '[E] is smaller than [S]': This is a valid assumption in the Michaelis-Menten model, as it allows the simplification that substrate concentration remains approximately constant during the reaction.

Conclude that the correct answer is the statement that does not align with the assumptions of the Michaelis-Menten equation, which is 'The rate of ES formation = to rate of P formation.'