The catalytic mechanism of an enzyme found in the mitochondrial matrix (pH = 7.8) depends on an active site Lys residue (pKa = 9.5) that acts as a general acid. Mutation of a neighboring residue alters  the microenvironment of the Lys side chain so that its pKa shifts from 9.5 to 7.4.  (a) Calculate the ratio of protonated to deprotonated Lys at pH 7.8 for the normal and mutant enzyme.   (b) Would you expect the mutation to increase or decrease the reaction rate? Explain your answer. (c) Lys is a classified as a basic amino acid, but it commonly acts as an acid catalyst in biochemical reactions. Explain this paradox.

Biochemistry
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Chapter1: Biochemistry: An Evolving Science
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The catalytic mechanism of an enzyme found in the mitochondrial matrix (pH = 7.8) depends on an active site Lys residue (pKa = 9.5) that acts as a general acid. Mutation of a neighboring residue alters
 the microenvironment of the Lys side chain so that its pKa shifts from 9.5 to 7.4. 
(a) Calculate the ratio of protonated to deprotonated Lys at pH 7.8 for the normal and mutant enzyme.
  (b) Would you expect the mutation to increase or decrease the reaction rate? Explain your answer.
(c) Lys is a classified as a basic amino acid, but it commonly acts as an acid catalyst in biochemical reactions. Explain this paradox.

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