Fig 5.

Insights from the MaxEnt model applied to de novo Kemp eliminase. (A) Kemp eliminase adopts the TIM-barrel scaffold of a natural synthase; its active center is modified to accommodate a new substrate. (B) Mutations on the Kemp eliminase scaffold show a correlation between $E(\mathit{S})$ and stability, evidenced by a Pearson’s correlation value of −0.77. (C) Mutations in the catalytically active remote region correlate their $E(\mathit{S})$ values with enzyme activity, indicated by a Pearson’s correlation value of −0.89. (The data used to generate this figure were sourced from Ref (65).)