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

Which of the following binds most tightly to the active site of an enzyme?

Substrate

Competitive inhibitor

Transition state analog

Product

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Verified step by step guidance

Understand the concept of enzyme active sites: Enzymes have specific regions called active sites where substrates bind and undergo chemical reactions. The binding affinity depends on the molecular structure and interactions between the enzyme and the molecule.

Learn about the transition state: The transition state is the high-energy intermediate formed during the conversion of a substrate into a product. Enzymes stabilize this state to lower the activation energy of the reaction.

Explore the role of transition state analogs: Transition state analogs are molecules that mimic the structure of the transition state but are stable and do not undergo the reaction. They bind very tightly to the enzyme's active site because the enzyme is designed to stabilize the transition state.

Compare binding affinities: Substrates, products, and competitive inhibitors bind to the active site, but their binding is generally weaker compared to transition state analogs. Substrates and products have lower affinity because they are not as complementary to the active site as the transition state. Competitive inhibitors bind to the active site but do not mimic the transition state as effectively as transition state analogs.

Conclude that transition state analogs bind most tightly: Since enzymes are optimized to stabilize the transition state, transition state analogs have the highest binding affinity to the active site compared to substrates, products, or competitive inhibitors.