Extended Data Fig. 5: Rate constants of the hydrolysis of fluorescein 2-phenylacetate catalysed by small-molecule nucleophilic catalysts. | Nature

Extended Data Fig. 5: Rate constants of the hydrolysis of fluorescein 2-phenylacetate catalysed by small-molecule nucleophilic catalysts.

From: Design and evolution of an enzyme with a non-canonical organocatalytic mechanism

Extended Data Fig. 5

ac, Linear plots showing the rate of hydrolysis of fluorescein 2-phenylacetate catalysed by 3-methylhistidine (Me-His) kMe-His = 0.35 M−1 s−1, R2 = 0.99) (a), dimethylaminopyridine (kDMAP = 1.13 M−1 s−1, R2 = 0.99) (b) and N-methylimidazole (kNMI = 1.16 M−1 s−1, R2 = 0.99) (c). d, Linear plot showing the rate of uncatalysed fluorescein 2-phenylacetate hydrolysis (kobs = 5.9 × 10−4 min−1, R2 = 0.98). Data are mean ± s.d. of measurements made in triplicate.

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