Step 1: Michaelis-Menten equation. The Michaelis-Menten equation is given by: \[ v = \frac{V_{\text{max}} \cdot [S]}{K_m + [S]} \] where: - \( v \) is the reaction rate, - \( V_{\text{max}} \) is the maximum rate, - \( [S] \) is the substrate concentration, - \( K_m \) is the Michaelis constant (substrate concentration at which the reaction rate is half of \( V_{\text{max}} \)).
Step 2: Condition when \( K_m = C \). When \( [S] = K_m \): \[ v = \frac{V_{\text{max}} \cdot K_m}{K_m + K_m} = \frac{V_{\text{max}}}{2} \] This shows that the rate of the process is equal to half of the maximum rate (\( V_{\text{max}} \)) when the substrate concentration equals the Michaelis constant (\( K_m \)).
Step 3: Comparison with other options. - Option \( (B) \): Zero-order kinetics occur when \( [S] \gg K_m \).
- Option \( (C) \): Constant rate occurs in zero-order kinetics.
- Option \( (D) \): First-order elimination occurs when \( [S] \ll K_m \).
Conclusion: The correct answer is \( (A) \).

| List I Name of Vitamin | List II Functions of Vitamins | ||
| A | Riboflavin | I | The electron acceptor for isocitrate dehydro- genase |
| B | Niacin | II | Decarboxylation of alpha-ketoglutarate dehydrogenas |
| C | Thiamine | III | Part of coenzyme A |
| D | Pantothenic acid | IV | Cofactor for succinate dehydrogenase |
| V | Enzyme activity regulator, such as for protein kinase C |
List I | List II | ||
|---|---|---|---|
| A | \(\Omega^{-1}\) | I | Specific conductance |
| B | \(∧\) | II | Electrical conductance |
| C | k | III | Specific resistance |
| D | \(\rho\) | IV | Equivalent conductance |
List I | List II | ||
|---|---|---|---|
| A | Constant heat (q = 0) | I | Isothermal |
| B | Reversible process at constant temperature (dT = 0) | II | Isometric |
| C | Constant volume (dV = 0) | III | Adiabatic |
| D | Constant pressure (dP = 0) | IV | Isobar |