Biochemistry Quiz
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Triose phosphate isomerase catalyzes the interconversion of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate through an enediolate intermediate. The enzyme achieves near diffusion-limited catalysis (kcat/Km ≈ 10⁸ M⁻¹s⁻¹). Glu165 acts as a general base to abstract a proton, while His95 stabilizes the intermediate. A flexible loop closes over the active site upon substrate binding. Which catalytic strategy is MOST critical for achieving this extraordinary catalytic efficiency?
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