Table of contents

1. A Review of General Chemistry5h 5m
2. Molecular Representations1h 14m
3. Acids and Bases2h 46m
4. Alkanes and Cycloalkanes4h 17m
5. Chirality3h 39m
6. Thermodynamics and Kinetics1h 22m
7. Substitution Reactions1h 48m
8. Elimination Reactions2h 30m
9. Alkenes and Alkynes2h 9m
10. Addition Reactions3h 19m
11. Radical Reactions1h 58m
12. Alcohols, Ethers, Epoxides and Thiols2h 42m
13. Alcohols and Carbonyl Compounds2h 17m
14. Synthetic Techniques1h 26m
15. Analytical Techniques:IR, NMR, Mass Spect7h 3m
16. Conjugated Systems6h 13m
17. Ultraviolet Spectroscopy51m
18. Aromaticity2h 34m
19. Reactions of Aromatics: EAS and Beyond5h 1m
20. Phenols55m
21. Aldehydes and Ketones: Nucleophilic Addition4h 56m
22. Carboxylic Acid Derivatives: NAS2h 51m
23. The Chemistry of Thioesters, Phophate Ester and Phosphate Anhydrides1h 10m
24. Enolate Chemistry: Reactions at the Alpha-Carbon1h 53m
25. Condensation Chemistry2h 9m
26. Amines1h 43m
27. Heterocycles2h 0m
28. Carbohydrates5h 53m
29. Amino Acids4h 20m
30. Peptides and Proteins2h 42m
31. Catalysis in Organic Reactions1h 30m
32. Lipids 2h 50m
33. The Organic Chemistry of Metabolic Pathways2h 52m
34. Nucleic Acids1h 32m
35. Transition Metals6h 14m
36. Synthetic Polymers1h 49m

3. Acids and Bases

Organic Chemistry Reactions

Organic Chemistry

3. Acids and Bases

Organic Chemistry Reactions

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Multiple Choice

Which of the following statements is true regarding competitive enzyme inhibition in organic chemistry reactions?

Competitive inhibitors bind to the active site of the enzyme, preventing substrate binding.

Competitive inhibitors decrease the enzyme's affinity for the substrate, lowering Km.

Competitive inhibitors bind to an allosteric site, altering the enzyme's shape.

Competitive inhibitors increase the maximum reaction rate (Vmax) of the enzyme.

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Verified step by step guidance

Understand the concept of competitive inhibition: In competitive inhibition, the inhibitor competes with the substrate for binding to the active site of the enzyme.

Identify the effect on enzyme kinetics: Competitive inhibitors increase the apparent Km (Michaelis constant) because they decrease the enzyme's affinity for the substrate, but they do not affect the Vmax (maximum reaction rate).

Clarify the binding site: Competitive inhibitors bind to the active site of the enzyme, not an allosteric site. This is a key characteristic that differentiates competitive inhibition from non-competitive or allosteric inhibition.

Analyze the given statements: The statement 'Competitive inhibitors bind to the active site of the enzyme, preventing substrate binding' is true, as it aligns with the definition of competitive inhibition.

Evaluate the other statements: The statement 'Competitive inhibitors bind to an allosteric site, altering the enzyme's shape' is incorrect for competitive inhibition, and 'Competitive inhibitors increase the maximum reaction rate (Vmax) of the enzyme' is also incorrect, as Vmax remains unchanged in competitive inhibition.