Please help :)
the ability of chymotrypsin to enhance cleavage of the peptide bond is facilitated by the catalytic triad and its nucleophilic serine. Provide a detailed explanation for the observation that a mutant form of chymotrypsin where the catalytic serine is mutated to an alanine is still able to promote peptide bond cleavage several orders of magnitude faster than the uncatalyzed reaction. Be sure to include relevant reaction coordinate diagrams in your answer (10 marks).
An answer & explanation would be greatly appreciated, thank you so much :)
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