GATE BT 2025 • Q49 MSQ • 2 Marks

Section 2: General Biotechnology

Bioenergetics and Metabolism

Subtopic: Thermodynamics & ATP Bioenergetics

Question Statement:

Which of the following statements is/are true regarding the effect of the concentration of metabolic intermediates on glycolysis in erythrocytes?

Options:

  • (A) Increased AMP levels stimulate glycolysis
  • (B) Increased citrate inhibits glycolysis
  • (C) Increased glucose 6-phosphate inhibits glycolysis
  • (D) Increased fructose 1,6-bisphosphate stimulates glycolysis

Official Answer Key:

A;B;D

Step-by-Step Solution & Explanation

### **Official Solution & Concept Analysis (GATE BT 2025 Q.49)** **1. Governing Concept**: - **Topic**: Enzyme Kinetics & Michaelis-Menten Mechanism - In uninhibited Michaelis-Menten kinetics: $v_0 = \frac{V_{\max} [S]}{K_m + [S]} = \frac{k_{\text{cat}} [E]_t [S]}{K_m + [S]}$ - $V_{\max} = k_{\text{cat}} [E]_t$: Proportional to total enzyme concentration. - $K_m$: Intrinsic kinetic constant reflecting substrate affinity (independent of $[E]_t$). - At $[S] \ll K_m$ (first-order regime): $v_0 \approx \left(\frac{V_{\max}}{K_m}\right) [S]$; velocity depends linearly on substrate concentration. - At $[S] \gg K_m$ (zero-order regime): $v_0 \approx V_{\max}$; reaction rate becomes independent of substrate concentration. **2. Option Analysis**: - **Option (A) is CORRECT**: $V_{\max}$ is directly proportional to the total enzyme concentration ($[E]_t$). - **Option (B) is CORRECT**: At high substrate concentrations ($[S] \gg K_m$), the reaction velocity is zero-order with respect to substrate and independent of $[S]$. - **Option (C) is INCORRECT**: $K_m$ is an intensive property of the enzyme-substrate pair and does not depend on enzyme concentration. - **Option (D) is CORRECT**: At low substrate concentrations ($[S] \ll K_m$), reaction rate exhibits first-order dependence on $[S]$. **3. Final Answer**: - **Correct Options**: **A, B, D**

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