. 2014 Jan 17;53(5):881–894. doi: 10.1021/bi401583f

Table 2. Isotope Effects for Steady-State Reactions of Benzyl Alcohol and Benzaldehyde Catalyzed by ADHs^a.

isotope effect	wild type^b	V207A	V203A^c
^DV₁/E_t	1.2 ± 0.1	1.7 ± 0.2	3.4 ± 0.2
^DV₁/(E_tK_b)	2.6 ± 0.8	2.7 ± 0.4	4.1 ± 0.6
^DV₁/(E_tK_a)	0.8 ± 0.2	1.1 ± 0.5	2.6 ± 0.7
^DV₂/E_t	1.2 ± 0.1	1.1 ± 0.1	1.1 ± 0.1
^DV₂/(E_tK_p)	2.6 ± 0.2	2.7 ± 0.4	3.1 ± 0.5
^DV₂/(E_tK_q)	1.0 ± 0.1	0.9 ± 0.1	0.75 ± 0.12

Kinetic constants were determined at 25 °C in 33 mM sodium phosphate and 0.25 mM EDTA buffer (pH 8.0). The superscript D represents the ratio of kinetic constants with protio and deutero substrates.

Natural wild-type enzyme.

From ref (37).

Table 2. Isotope Effects for Steady-State Reactions of Benzyl Alcohol and Benzaldehyde Catalyzed by ADHsa.

Table 2. Isotope Effects for Steady-State Reactions of Benzyl Alcohol and Benzaldehyde Catalyzed by ADHs^a.