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5. pH Optimum of Lysozyme The enzymatic activity of lysozyme is optimal at pH 5.2. The active site of lysozyme contains two amino acid residues essential for catalysis, Glu³* and Asp². The pK, values of the carboxyl side chains of these two residues are 5.9 and 4.5, respectively. (a) What is the ionization state (protonated or deprotonated) of each residue at the pH optimum of lysozyme? (b) How can the ionization states of these two amino acid residues explain the pH-activity profile of lysozyme shown below? (c) Lysozyme destroys bacterial cell walls by hydrolyzing a glycosidic linkage between two sugars moieties. Based on your answers to parts (a) and (b), predict the possible catalytic roles of Glu³5 and Asp". 100 50 4 6 10 pH Activity (% of maximal)

5. pH Optimum of Lysozyme The enzymatic activity of lysozyme is optimal at pH 5.2. The active site of lysozyme contains two amino acid residues essential for catalysis, Glu³* and Asp². The pK, values of the carboxyl side chains of these two residues are 5.9 and 4.5, respectively. (a) What is the ionization state (protonated or deprotonated) of each residue at the pH optimum of lysozyme? (b) How can the ionization states of these two amino acid residues explain the pH-activity profile of lysozyme shown below? (c) Lysozyme destroys bacterial cell walls by hydrolyzing a glycosidic linkage between two sugars moieties. Based on your answers to parts (a) and (b), predict the possible catalytic roles of Glu³5 and Asp". 100 50 4 6 10 pH Activity (% of maximal)

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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5. pH Optimum of Lysozyme The enzymatic activity of lysozyme is optimal at pH 5.2. The active site of lysozyme contains two amino acid residues essential for catalysis, Glu³* and Asp². The pK, values of the carboxyl side chains of these two residues are 5.9 and 4.5, respectively. (a) What is the ionization state (protonated or deprotonated) of each residue at the pH optimum of lysozyme? (b) How can the ionization states of these two amino acid residues explain the pH-activity profile of lysozyme shown below? (c) Lysozyme destroys bacterial cell walls by hydrolyzing a glycosidic linkage between two sugars moieties. Based on your answers to parts (a) and (b), predict the possible catalytic roles of Glu³5 and Asp". 100 50 4 6 10 pH Activity (% of maximal)
Transcribed Image Text:5. pH Optimum of Lysozyme The enzymatic activity of lysozyme is optimal at pH 5.2. The active site of lysozyme contains two amino acid residues essential for catalysis, Glu³* and Asp². The pK, values of the carboxyl side chains of these two residues are 5.9 and 4.5, respectively. (a) What is the ionization state (protonated or deprotonated) of each residue at the pH optimum of lysozyme? (b) How can the ionization states of these two amino acid residues explain the pH-activity profile of lysozyme shown below? (c) Lysozyme destroys bacterial cell walls by hydrolyzing a glycosidic linkage between two sugars moieties. Based on your answers to parts (a) and (b), predict the possible catalytic roles of Glu³5 and Asp". 100 50 4 6 10 pH Activity (% of maximal)
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