Introduction to Enzymology - Enzymology | Lecture Notes - YNetStudyHub
Enzymology

Introduction to Enzymology

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Overview of enzymes, their functions, classification, and importance in biological systems.

Introduction to Enzymology – Study Notes


1. What Is Enzymology?

  • Definition: Enzymology is the branch of biochemistry that studies enzymes – the protein (or RNA) catalysts that accelerate biochemical reactions in living cells.
  • Scope:
    • Enzyme structure & classification
    • Kinetic behavior & mechanisms
    • Regulation & inhibition
    • Methods for purification, assay, and characterization

2. Basic Properties of Enzymes

Property Description Typical Example
Biological catalysts Lower activation energy (ΔG‡) without being consumed. Hexokinase phosphorylates glucose.
Specificity Recognize particular substrates (or a group of related substrates). Lactase hydrolyzes β‑galactosides.
Efficiency Turnover numbers (k_cat) can reach 10⁶ s⁻¹ for diffusion‑limited enzymes. Catalase decomposes H₂O₂ ~10⁷ s⁻¹.
Regulation Activity modulated by effectors, covalent modification, or changes in expression. Phosphofructokinase (PFK) allosterically activated by ADP.
Reversibility Many enzymes catalyze reversible reactions; direction depends on cellular conditions. Malate dehydrogenase (oxaloacetate ↔ malate).
Optimal conditions Each enzyme has an optimal pH, temperature, and ionic strength. Pepsin: pH ≈ 2; DNA polymerase: 37 °C.

3. Enzyme Structure

  1. Primary structure – linear amino‑acid sequence.
  2. Secondary structure – α‑helices, β‑sheets (stabilized by hydrogen bonds).
  3. Tertiary structure – overall 3‑D fold; active site formed by residues from different regions.
  4. Quaternary structure – assembly of multiple polypeptide subunits (e.g., hemoglobin, α₂β₂).

Key concept: Active site – a pocket/cleft where substrate binds; often contains catalytic residues (e.g., Ser‑His‑Asp triad in serine proteases).


4. Enzyme Classification (IUBMB System)

EC Class Reaction Type Example
EC 1 Oxidoreductases Alcohol dehydrogenase
EC 2 Transferases Hexokinase (phosphate transfer)
EC 3 Hydrolases Lipase (ester bond hydrolysis)
EC 4 Lyases Fumarase (C–C bond cleavage)
EC 5 Isomerases Triosephosphate isomerase
EC 6 Ligases (synthetases) DNA ligase
EC 7 Translocases (2021 addition) ATP synthase (proton translocation)

Mnemonic: Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, Ligases, Translocases.


5. Enzyme Kinetics

5.1 Michaelis–Menten Model

[ v = \frac{V_{\max}[S]}{K_m + [S]} ]

  • v – initial reaction velocity
  • **V
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Unit Syllabus 9 Topics
Introduction to Enzymology
Enzyme Structure and Function
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Enzyme Kinetics
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Enzyme Regulation
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Enzyme Mechanisms
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Enzymes in Biotechnology
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Enzymes in Disease
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Enzymes in Drug Development
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Enzymes in the Environment
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