12. Mechanism of Enzyme Action | Lock & Key Model, Induced fit, substrate strain, MOA catalysis
Awesome Biochemistry
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12. Mechanism of Enzyme Action | Lock & Key Model, Induced fit, substrate strain, MOA catalysis
1 946 просмотров · 1 год назад
Awesome Biochemistry
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1 946 просмотров · 1 год назад
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• Enzyme
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Mechanism of Enzyme Action – Lock & Key Model, Induced Fit, Catalysis Explained! 🧪🔬
📌 In this video, you’ll learn:
How enzymes catalyze reactions by lowering activation energy (ΔG‡).
3 models of enzyme-substrate binding: Fischer’s Lock & Key, Koshland’s Induced Fit, and Substrate Strain Theory.
4 mechanisms of enzyme catalysis: Acid-Base, Covalent, Proximity, and Strain Catalysis.
Real-world examples (e.g., Serine Proteases, Lysozyme, Ribonuclease).
📖 Detailed Breakdown:
1️⃣ Energy Changes in Reactions: Transition states, activation energy, and how enzymes speed up reactions without altering equilibrium.
2️⃣ Enzyme-Substrate Complex Formation:
Fischer’s Template Theory (1894): Rigid active sites & specificity.
Koshland’s Induced Fit (1958): Flexible enzymes & conformational changes.
Substrate Strain Theory: Enzyme-induced substrate destabilization.
3️⃣ Catalysis Mechanisms: How amino acid side chains (e.g., Histidine, Serine) facilitate reactions.
🔥 Key Questions Answered:
Why doesn’t an enzyme change ΔG of a reaction?
What’s the difference between lock-and-key vs. induced fit?
How do allosteric regulators affect enzyme action?
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Index:
00:00 – Introduction
01:25 – Energy changes in reaction
09:18 – Fischer’s Templet theory
12:18 – Koshland’s Induced Fit theory
14:17 – Substrate Strain Theory
16:15 – 4 Catalysis Mechanisms (Acid-Base, Covalent, Proximity, Strain)
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