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 Inhibition

GOB Chemistry

19. Enzymes

Enzyme Inhibition

Previous problemNext problem

4:44 minutes

Problem 58b

Textbook Question

The text discusses three forms of enzyme inhibition: uncompetitive inhibition, competitive inhibition, and irreversible inhibition.
b. What kinds of bonds are formed between an enzyme and each of these three kinds of inhibitors?

Verified step by step guidance

Understand the three types of enzyme inhibition: Competitive inhibition occurs when an inhibitor competes with the substrate for the active site of the enzyme. Uncompetitive inhibition occurs when the inhibitor binds only to the enzyme-substrate complex. Irreversible inhibition involves the permanent inactivation of the enzyme by the inhibitor.

For competitive inhibition, the bonds formed between the enzyme and the inhibitor are typically weak, non-covalent interactions such as hydrogen bonds, ionic bonds, or van der Waals forces. These interactions are reversible.

For uncompetitive inhibition, the inhibitor binds to the enzyme-substrate complex, often forming non-covalent bonds such as hydrogen bonds or ionic interactions. These bonds are also reversible.

For irreversible inhibition, the inhibitor forms strong covalent bonds with the enzyme, permanently inactivating it. This type of inhibition is not reversible under normal physiological conditions.

Summarize the bond types: Competitive and uncompetitive inhibitors form reversible, non-covalent bonds, while irreversible inhibitors form strong, covalent bonds with the enzyme.

Verified video answer for a similar problem:

This video solution was recommended by our tutors as helpful for the problem above

Video duration:

Play a video:

Was this helpful?

Key Concepts

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

Uncompetitive Inhibition

Uncompetitive inhibition occurs when an inhibitor binds to the enzyme-substrate complex, preventing the complex from releasing products. This type of inhibition typically involves non-covalent interactions, such as hydrogen bonds and van der Waals forces, which stabilize the inhibitor's binding to the enzyme-substrate complex.

Competitive Inhibition

Competitive inhibition happens when an inhibitor competes with the substrate for binding to the active site of the enzyme. The bonds formed in this case are usually non-covalent, including hydrogen bonds and ionic interactions, allowing the inhibitor to temporarily occupy the active site and block substrate access.

Irreversible Inhibition

Irreversible inhibition involves the formation of a stable, covalent bond between the inhibitor and the enzyme, permanently inactivating the enzyme. This type of inhibition often modifies key amino acid residues in the active site, leading to a long-lasting effect on enzyme activity.

Watch next

Master Enzyme Inhibition Concept 1 with a bite sized video explanation from Jules

Start learning

Related Videos

Related Practice

Textbook Question

Indicate whether each of the following describes a competitive or a noncompetitive inhibitor.

c. The inhibitor competes with the substrate for the active site.

1027

views

Multiple Choice

Which of the following inhibitors could be a reversible competitive inhibitor for acetylcholinesterase if its substrate is acetylcholine?

814

views

Textbook Question

How can you distinguish between a competitive inhibitor and an uncompetitive inhibitor experimentally?

1242

views

Textbook Question

Why are irreversible enzyme inhibitors referred to as poisons?

1469

views

Textbook Question

What kind of inhibition (uncompetitive, competitive, or irreversible) is present in each of the following:

a. Penicillin is used to treat certain bacterial infections. Penicillin is effective because it binds to the enzyme glycopeptide transpeptidase and does not dissociate.

1098

views

Textbook Question

What kind of inhibition (uncompetitive, competitive, or irreversible) is present in each of the following:

c. The antibiotic deoxycycline inhibits the bacterial enzyme collagenase, slowing bacterial growth. Deoxycycline does not fit into the active site of collagenase and binds elsewhere on the enzyme.

1644

views

Textbook Question

One mechanism by which lead exerts its poisonous effect on enzymes can be stopped by chelation therapy with EDTA. Describe this type of lead poisoning and explain why it is reversible.

1378

views

Textbook Question

What kind of reaction product might be a competitive inhibitor for the enzyme that catalyzes its formation?

1088

views

Show more practices