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

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Multiple Choice

Each enzyme only has one specific substrate that will fit its active site. What is this concept called?

Lock and key model

Competitive inhibition

Induced fit model

Allosteric regulation

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Verified step by step guidance

Understand the concept of enzyme specificity: Enzymes are biological catalysts that speed up chemical reactions. Each enzyme has an active site, which is a specific region where the substrate binds. The shape and chemical properties of the active site determine which substrate can bind to it.

Review the 'Lock and Key Model': This model suggests that the enzyme's active site has a specific shape that perfectly matches the substrate, similar to how a key fits into a lock. This explains the high specificity of enzymes for their substrates.

Consider the 'Induced Fit Model': This model proposes that the enzyme's active site is flexible and changes shape slightly to accommodate the substrate when it binds. This is a refinement of the lock and key model and accounts for the dynamic nature of enzyme-substrate interactions.

Understand 'Competitive Inhibition': This occurs when a molecule similar in shape to the substrate competes for binding to the active site, preventing the substrate from binding and inhibiting the enzyme's activity.

Learn about 'Allosteric Regulation': This involves molecules binding to a site other than the active site (called the allosteric site), which can change the enzyme's shape and either enhance or inhibit its activity. This is different from the substrate binding directly to the active site.