The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pk values for the side-chain carboxyl groups on the two amino acids in solution are virtually identical. a) How can one carboxyl group be charged and the other uncharged in the active site of lysozyme? b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreases above and below this optimum? Glu35 NAG Asp52 Glu35 -C, Asp52 tri-NAG NAG

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Chapter1: Biochemistry: An Evolving Science
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. The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its
nonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pK
values for the side-chain carboxyl groups on the two amino acids in solution are virtually
identical.
a) How can one carboxyl group be charged and the other uncharged in the active site of
lysozyme?
b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreases
above and below this optimum?
Glu3s
NAG
Asp52
0-H
Glu35 -C
Asp52
tri-NAG
NAG
Transcribed Image Text:. The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pK values for the side-chain carboxyl groups on the two amino acids in solution are virtually identical. a) How can one carboxyl group be charged and the other uncharged in the active site of lysozyme? b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreases above and below this optimum? Glu3s NAG Asp52 0-H Glu35 -C Asp52 tri-NAG NAG
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