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. Author manuscript; available in PMC: 2017 Sep 14.
Published in final edited form as: J Am Chem Soc. 2016 Sep 1;138(36):11890–11895. doi: 10.1021/jacs.6b06843

Figure 6. Linear correlation between the proton affinity of KSI’s active site and the catalytic proficiency.

Figure 6

The catalytic proficiency improves linearly as the proton affinity of the enzyme (pKαE) approaches that of the intermediate (pKaI =10) (R2 = 0.99). The extra stabilization energy for barrier reduction is presumably due to the increased H-bond strength between the enzyme and the intermediate, which is estimated to be 6.3 ± 0.2 kcal/mol.