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 describes how a competitive inhibitor works in an enzyme-catalyzed reaction?

It binds to an allosteric site, changing the enzyme's shape and function.

It forms a covalent bond with the substrate, making it inactive.

It increases the enzyme's affinity for the substrate.

It binds to the active site of the enzyme, preventing substrate binding.

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Verified step by step guidance

Understand the role of enzymes: Enzymes are biological catalysts that speed up chemical reactions by lowering the activation energy. They have specific active sites where substrates bind to form enzyme-substrate complexes.

Define competitive inhibition: A competitive inhibitor is a molecule that resembles the substrate and competes for binding to the active site of the enzyme. This prevents the actual substrate from binding, thereby inhibiting the enzyme's activity.

Differentiate from other types of inhibition: Unlike non-competitive inhibitors, which bind to an allosteric site and change the enzyme's shape, competitive inhibitors do not alter the enzyme's structure but simply block the active site.

Consider the effect on enzyme kinetics: In the presence of a competitive inhibitor, the maximum reaction rate (Vmax) remains unchanged, but the apparent affinity of the enzyme for the substrate (Km) increases, as more substrate is needed to achieve half of Vmax.

Conclude with the correct description: A competitive inhibitor works by binding to the active site of the enzyme, preventing the substrate from binding and thus inhibiting the enzyme-catalyzed reaction.