. Author manuscript; available in PMC: 2011 Apr 27.

Published in final edited form as: Biochemistry. 2010 Apr 27;49(16):3487–3498. doi: 10.1021/bi100294m

Table 4.

Enantioselectivity of 2-butanone reduction by wild-type rS-HPCDH3, rS-HPCDH3 mutants, and rR-HPCDH1^a

Enzyme	no additions			+ 1 mM ethanesulfonate

	% (S)-2-butanol	% (R)-2-Butanol	ee (S)-2-butanol	% (S)-2-butanol	% (R)-2-butanol	ee (S)-2-butanol
rS-HPCDH3	99.2 ± 0.2	0.82 ± 0.15	98.36	98.0 ± 0.08	1.97 ± 0.08	96.06
rS-HPCDH3 R211A	99.4 ± 0.2	0.58 ± 0.22	98.84	99.4 ± 0.2	0.64 ± 0.15	98.72
rS-HPCDH3 K214A	91.6 ± 0.3	8.4 ± 0.31	83.18	90.9 ± 0.2	9.12 ± 0.20	81.76
rR-HPCDH1	71.9 ± 1.3	28.0 ± 1.3	43.88	92.7 ± 0.1	7.33 ± 0.05	85.34

All assays were performed in triplicate at 30 °C using 0.64 mg enzyme, 15 mM NADH, and 56 mM 2-butanone. Percent yields are reported as means ± standard deviations.