Overview of enzymes, their functions, classification, and importance in biological systems.
Introduction to Enzymology – Study Notes
| 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. |
Key concept: Active site – a pocket/cleft where substrate binds; often contains catalytic residues (e.g., Ser‑His‑Asp triad in serine proteases).
| 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.
[ v = \frac{V_{\max}[S]}{K_m + [S]} ]