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

Michaelis & Menten assumed that the initial reaction for an enzyme catalyzed reaction could be written as shown:

Using this, the rate/velocity of ES-complex breakdown can be expressed by:

k₁ ([E]_T – [ES]).

k₁ ([E]_T – [ES])[S].

k₂ [ES].

k_-1 [ES] + k₂ [ES].

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Verified step by step guidance

Understand the Michaelis-Menten model: It describes the rate of enzymatic reactions by relating reaction rate to substrate concentration. The model assumes the formation of an enzyme-substrate complex (ES) as an intermediate step.

Identify the reaction steps: The enzyme (E) binds to the substrate (S) to form the enzyme-substrate complex (ES). This complex can either dissociate back to E and S or proceed to form the product (P) and release the enzyme.

Write the rate equations: The formation of ES is governed by the rate constant k1, and its breakdown is governed by k-1 (dissociation back to E and S) and k2 (formation of product P).

Express the breakdown of ES: The breakdown of the ES complex can be expressed as the sum of the rates of its dissociation and conversion to product, which is given by the equation: v = k-1 [ES] + k2 [ES].

Interpret the equation: The term k-1 [ES] represents the rate of ES dissociating back to E and S, while k2 [ES] represents the rate of ES converting to product P. Together, they describe the total rate of ES breakdown.