. 2014 May 1;136(21):7643–7654. doi: 10.1021/ja413174b

Table 3. Solvent Isotope Effects on the Initial Rates of Product Formation from 5(10)-EST with Semisynthetic KSIs under Subsaturating and Saturating Conditions^a.

residue at position 16	v_H₂O/v_D₂O (subsaturating)	v_H₂O/v_D₂O (saturating)
Tyr (WT)	0.99 ± 0.12	0.94 ± 0.05
2-F-Tyr	1.04 ± 0.13	1.00 ± 0.03
3-F-Tyr	1.03 ± 0.09	1.10 ± 0.05
2,6-F₂-Tyr	1.09 ± 0.12	1.03 ± 0.01

Conditions: 40 mM potassium phosphate, 1 mM EDTA, 2% DMSO (v/v), pH 7.2 (H₂O) or pD 7.6 (D₂O). Standard deviations are from 6 to 12 (subsaturating) or 2 to 3 (saturating) independent experiments. Subsaturating data were collected with 2.3, 4.7, 9.4, 18.8, or 37.5 μM substrate, and saturating data were collected with 300 μM substrate. Enzyme concentrations were varied over a 3-fold range with 2.3, 4.7, and 300 μM substrate.

Table 3. Solvent Isotope Effects on the Initial Rates of Product Formation from 5(10)-EST with Semisynthetic KSIs under Subsaturating and Saturating Conditionsa.

Table 3. Solvent Isotope Effects on the Initial Rates of Product Formation from 5(10)-EST with Semisynthetic KSIs under Subsaturating and Saturating Conditions^a.