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Class 11 Biology Notes | Chapter 3: Enzymes (FBISE, Best for Exams)

Enzyme | Best 11th Class Biology Notes | Federal Board 

Chapter 3 : 

Enzymes


Enzymes

  • Metabolism = Sum of all chemical rxns in a cell.
  • Enzymes = Biological catalysts → ↑ rxn speed w/o consumption.

Properties:

✅ ↑ Speed of chemical rxns.
✅ Small qty required.
✅ pH & Temp sensitive.
✅ Specificity: Highly or slightly specific.
✅ Work in vivo & vitro.
✅ Some need cofactors for activity.
✅ ↓ Activation energy.
✅ No effect on equilibrium.

  • Payen & Persoz (19th century) → Discovered diastase, an enzyme digesting starch.

Enzyme Structure

  • Globular proteins (except ribozymes).
  • Ribozymes = RNA-based enzymes (e.g., peptidyl transferase).
  • Active Site = 3D cavity where rxn occurs.
    • Binding site = Holds substrate.
    • Catalytic site = Converts substrate → product.

Cofactors:

  • Holoenzyme = Enzyme + cofactor (active).
  • Apoenzyme = Enzyme w/o cofactor (inactive).
  • Pepsinogen → Pepsin (Activated in HCl).

Types of Cofactors

🔹 Inorganic (Activators) → Fe²⁺, Mg²⁺, Cu²⁺, Zn²⁺ (Detach after rxn).
🔹 Organic:

  • Coenzymes (Vitamin derivatives) → ATP, NAD⁺, FAD⁺.
  • Prosthetic groups (Permanently attached) → Heme in cytochromes.

Mechanism of Enzyme Action

  1. E + S → ES → EP → E + P
  2. Enzyme alters pH, charge, bond stress → Easier rxn.

Models of Action

  • Lock & Key (Fischer, 1894) → Fixed shape active site, highly specific.

  •  Induced Fit (Koshland, 1959) → Flexible active site, molds to substrate.


Activation Energy (Ea)

  • Enzymes ↓ Ea, making rxns possible w/o excessive heat.
  • Rxn Pathway:
    A + E → AE Complex + B → AB + E

Factors Affecting Enzymes

Temp:

  • Optimum: Max activity (~37°C humans, ~70°C bacteria).
  • Too high → Denaturation.
  • Too low → Inactive but reversible.

pH:

  • Optimum pH varies (e.g., Pepsin = 2, Trypsin = 8).
  • Extreme pH → Denaturation.

[Enzyme] → Rxn rate ↑ (until substrate saturation).


[Substrate] ↑ → Rxn rate ↑, but plateaus at Vmax.


Enzyme Inhibition

❌ Competitive (Reversible)

  • Inhibitor competes for active site.
  • ExampleMalonate inhibits succinate dehydrogenase.

 Non-Competitive (Reversible or Irreversible)

  • Binds allosteric site, alters active site shape.
  • ExampleCyanide inhibits cytochrome oxidase.

🔄 Feedback Inhibition

  • End product inhibits 1st enzyme in pathway.
  • ExampleThreonine inhibits 1st enzyme in its synthesis pathway.

Enzyme Classification (IUB 1961)

1️⃣ Oxidoreductases (Redox rxns) → Cytochrome oxidase.
2️⃣ Transferases (Transfer groups) → Hexokinase.
3️⃣ Hydrolases (Hydrolysis) → Pepsin, trypsin.
4️⃣ Lyases (Break bonds w/o H₂O) → Histidine decarboxylase.
5️⃣ Isomerases (Rearrange molecules) → Phosphohexose isomerase.
6️⃣ Ligases (Join molecules using ATP) → DNA ligase.


Enzyme Uses

🏭 Industry:

  • Food → Amylase (syrups), Protease (meat tenderizing).
  • Detergents → Lipase & Protease (stain removal).
  • Paper/Leather → Ligninase (bleaching), Protease (hide processing).

🏥 Medicine:

  • Diagnosis → ALT, AST (Liver), Troponin (Heart).
  • Treatment → Streptokinase (Clot dissolving), Asparaginase (Cancer).

🧬 Genetic Engineering:

  • DNA cutting → Restriction enzymes.
  • DNA joining → Ligases.
  • DNA copying → Polymerases (PCR).