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0.4 0.6 [S] (mi)

17. The Effects of Reversible Inhibitors Derive the expression for the effect of a reversible inhibitor on observed Km (apparent Km = aKm/a'). Start with Equation 6-30 and the statement that apparent Km is equivalent to the [S] at which Vo = Vmax/2a .

18. pH Optimum of Lysozyme The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and Asp52. The pKa values of the carboxyl side chains of these residues are 5.9 and 4.5, respectively. What is the ionization state (protonated or deprotonated) of each residue at pH 5.2, the pH optimum of lysozyme? How can the ionization states of these residues explain the pH-activity profile of lysozyme shown below?

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