Is strong hydrogen bonding in the transition state enough to account for the observed rate acceleration in a mutant of papain?

Abstract excerpt

Nitriles are good inhibitors for the cysteine protease papain. However, a single amino acid mutation (Gln-19 --> Glu-19) in the active site makes the mutant enzyme a good catalyst for nitrile hydrolysis. A theoretical approach was used to examine the differential transition state stabilization in the papain mutant relative to the wild-type enzyme. Based on this study, we concluded that strong hydrogen bonding in...

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