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Question 1 Describe transition state theory and how it applies to enzyme catalysis. Why is a transition-state analog not necessarily the same as a
Question 1
Describe transition state theory and how it applies to enzyme catalysis. Why is a transition-state analog not necessarily the same as a competitive inhibitor?
Question 2
Why does pH affect the activity of an enzyme? 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: Glu35 and Asp52. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5, respectively. What is the ionization state of each residue at the pH optimum of lysozyme? How can the ionization states of these two amino acid residues explain the pH-activity profile of lysozyme?
