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

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 16P

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