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-Substrate Complex

Biochemistry

6. Enzymes and Enzyme Kinetics

Enzyme-Substrate Complex

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Multiple Choice

The enzyme that catalyzes the reaction shown should have which of the following properties at its active site?

A complementary shape and chemical environment to bind the substrate specifically and stabilize the transition state

A rigid structure that prevents any conformational changes upon substrate binding

A non-polar environment that excludes all water molecules

An active site that binds the product more tightly than the substrate

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Verified step by step guidance

Understand the role of an enzyme's active site: The active site is the region of the enzyme where the substrate binds and the chemical reaction occurs. It is specifically designed to interact with the substrate and stabilize the transition state, which lowers the activation energy required for the reaction.

Analyze the options provided: Evaluate each option based on the principles of enzyme function. For example, enzymes typically have a complementary shape and chemical environment to bind the substrate specifically and stabilize the transition state. This is crucial for catalysis.

Consider the importance of flexibility: Enzymes often undergo conformational changes upon substrate binding (induced fit model). A rigid structure that prevents conformational changes would hinder the enzyme's ability to stabilize the transition state effectively.

Evaluate the role of the environment: While some enzymes may have non-polar regions, excluding all water molecules is not a universal property of active sites. Many enzymes operate in aqueous environments and rely on water for certain catalytic mechanisms.

Assess substrate vs. product binding: Enzymes are designed to bind the substrate specifically and stabilize the transition state, but they should not bind the product more tightly than the substrate. Tight product binding could inhibit the release of the product and reduce the enzyme's efficiency.