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

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

Which of the following best describes the nature of enzyme and substrate binding in the formation of the enzyme-substrate complex?

It requires the hydrolysis of ATP.

It is a reversible, non-covalent interaction.

It involves only hydrophobic interactions.

It is an irreversible, covalent interaction.

Previous problemNext problem

Verified step by step guidance

Understand the concept of enzyme-substrate binding: Enzymes bind to substrates to form an enzyme-substrate complex, which is a key step in catalyzing biochemical reactions. This binding is typically reversible and involves non-covalent interactions.

Review the types of non-covalent interactions: These include hydrogen bonds, ionic bonds, van der Waals forces, and hydrophobic interactions. These interactions allow the enzyme to recognize and bind the substrate specifically.

Clarify why ATP hydrolysis is not required: ATP hydrolysis is an energy-releasing process used in other cellular activities, but enzyme-substrate binding does not require ATP hydrolysis as it relies on the intrinsic affinity between the enzyme and substrate.

Explain why the interaction is reversible: Enzyme-substrate binding is reversible to allow the enzyme to release the product after the reaction. This reversibility is crucial for the enzyme to participate in multiple catalytic cycles.

Discuss why covalent or hydrophobic-only interactions are incorrect: Covalent interactions would make the binding irreversible, which is not typical for enzyme-substrate complexes. Hydrophobic interactions may play a role but are not the sole type of interaction involved in binding.