The enzymatic activity of lysosome is optimal at pH 5.2 and decreases above below this pH value contains two amino acid residue in the act of site essential for catalysis
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The enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu-35 and Asp-52. The pKa value for the carbonyl side chains of these two residues are 6.2 and 3.8, respectively. Questions: (1) What is the ionization state of each residue at the pH optimum (pH=5.2) of lysozyme? (2) Why does lysozyme activity decrease when pH=7.0?
Adi S.
The enzymatic activity of lysozyme is optimal at pH 5.2, but decreases above or below this pH. The pKa for the carboxyl side chains of Glu35 and Asp52 at the active site of lysozyme are 5.9 and 4.5, respectively. At pH 5.2: Glu35 is protonated and serves as a general acid to catalyze the reaction. Asp52 is protonated and serves as a general acid to catalyzes the reaction. Both Glu35 and Asp52 are protonated. Both Glu35 and Asp52 are deprotonated. Glu35 forms a covalent bond with the reaction intermediate.
Madhur L.
The active site of lysozyme contains two amino acid residues essential for catalysis: Glu^{3 } and $\mathrm{Asp}^{52}$. The $\mathrm{p} K_{\mathrm{a}}$ 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 $\mathrm{pH} 5.2,$ the $\mathrm{pH}$ optimum of Iysozyme? How can the ionization states of these residues explain the pH-activity profile of lysozyme shown below? (GRAPH CAN'T COPY)
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