3. Which of the following statements about enzyme catalysis is not true? (A) the

Question

3. Which of the following statements about enzyme catalysis is not true? (A) the transition state is stabilized due to the specificity of the active site for the substrate (B) serine proteases use electrostatic interactions to catalyze peptide bond cleavages (C) zymogens are not properly shaped forms of enzymes (D) lysozyme requires a deprotonated Glu in the active site for catalytic transformation (E) none of above. 4. In steady-state kinetics, the Michaelis constant (KM) can approximate the dissociation constant (Ks) for enzyme (E)-substrate (S) binding if (A) the enzyme-substrate complex (ES) remains constant in concentration (B) ES breakdown is faster than ES formation (C) chemical conversion is much slower than ES dissociation (D) substrate binding is much faster than chemical conversion (E) none of above since KM can not approach closely to Ks. 5. Which of the following is not true? (A) An enzyme inhibitor can be considered to be a lead compound when its inhibition constant (Ki) is in the order of 10- M (B) Irreversible enzyme inhibitors inhibit competitively (C) An enzyme is close to maximum efficiency when kcal/KM is near 108 M's-1 (D) Parallel lines on a Lineweaver-Burk plot suggest decrease in V max (E) none of above. (Vmax: maximum velocity; kcat: turnover number; KM. Michaelis constant)

Explanation / Answer

3. Since, the transition state of the enzyme is not stable, it change into the product soon. Hence, option a is not correct.

4. Michaelis constant is equal to dissociation constant when rate of formation of ES is equal to its dissociation . Hence, option a is correct .

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