Table of contents

1. Matter and Measurements4h 31m
2. Atoms and the Periodic Table5h 23m
3. Ionic Compounds2h 18m
4. Molecular Compounds2h 18m
5. Classification & Balancing of Chemical Reactions3h 17m
6. Chemical Reactions & Quantities2h 27m
7. Energy, Rate and Equilibrium3h 46m
8. Gases, Liquids and Solids3h 25m
9. Solutions4h 10m
10. Acids and Bases3h 29m
11. Nuclear Chemistry56m
BONUS: Lab Techniques and Procedures1h 38m
BONUS: Mathematical Operations and Functions47m
12. Introduction to Organic Chemistry1h 34m
13. Alkenes, Alkynes, and Aromatic Compounds2h 12m
14. Compounds with Oxygen or Sulfur1h 6m
15. Aldehydes and Ketones1h 1m
16. Carboxylic Acids and Their Derivatives1h 11m
17. Amines39m
18. Amino Acids and Proteins1h 51m
19. Enzymes1h 37m
20. Carbohydrates1h 41m
21. The Generation of Biochemical Energy2h 8m
22. Carbohydrate Metabolism2h 22m
23. Lipids2h 26m
24. Lipid Metabolism1h 45m
25. Protein and Amino Acid Metabolism1h 37m
26. Nucleic Acids and Protein Synthesis2h 54m

19. Enzymes

Enzyme Regulation: Allosteric Control

GOB Chemistry

19. Enzymes

Enzyme Regulation: Allosteric Control

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2:49 minutes

Problem 66

Textbook Question

Why do allosteric enzymes have two types of binding sites?

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Allosteric enzymes are specialized proteins that regulate biochemical pathways by responding to the needs of the cell. They have two types of binding sites: the active site and the allosteric site.

The active site is where the substrate binds and undergoes a chemical reaction. This is the site responsible for the enzyme's catalytic activity.

The allosteric site is a separate location on the enzyme where regulatory molecules, called allosteric effectors, bind. These effectors can either activate or inhibit the enzyme's activity.

When an allosteric effector binds to the allosteric site, it induces a conformational change in the enzyme's structure. This change can either enhance or reduce the enzyme's ability to bind to the substrate at the active site.

This dual binding site system allows allosteric enzymes to finely tune their activity in response to cellular signals, ensuring that metabolic pathways are efficiently regulated based on the cell's needs.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Allosteric Regulation

Allosteric regulation refers to the process by which an enzyme's activity is modulated by the binding of an effector molecule at a site other than the active site. This binding can induce conformational changes in the enzyme, enhancing or inhibiting its activity. Allosteric enzymes typically exhibit a sigmoidal kinetic response, reflecting their complex regulation.

Active Site vs. Allosteric Site

Allosteric enzymes possess two distinct types of binding sites: the active site, where substrate molecules bind to facilitate the enzymatic reaction, and the allosteric site, where regulatory molecules can bind. The interaction at the allosteric site can lead to changes in the enzyme's shape and function, allowing for fine-tuned control of metabolic pathways.

Cooperativity

Cooperativity is a phenomenon observed in allosteric enzymes where the binding of a substrate to one active site affects the binding affinity of additional substrate molecules to other active sites. This can result in increased efficiency of substrate conversion as more substrate molecules bind, illustrating the enzyme's ability to respond dynamically to changes in substrate concentration.

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