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The effect of pH on the activity of lysozyme

Description
E35 must be protonated to act as a general acid catalyst in the first step of the mechanism; thus, at pH values below 6.2 the ratio of [COOH]/[COO-] is greatest, favoring catalysis.

D52 must be deprotonated to interact with the oxocarbenium ion; thus, at pH values above 3.7 the ratio of [COO-]/[COOH] is greatest, favoring catalysis.

These two boundary requirements give rise to the observed pH optimum (~5) where both protonated E35 and deprotonated D52 are abundant.
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