. 2003 Mar;12(3):468–479. doi: 10.1110/ps.0221603

Table 1.

Kinetic constants for mutant enzymes

Kinetic constants	Wild-type	E60A	E60D
K_a, μM	83	140	11
K_b, mM	0.22	0.43	0.20
K_ia, μM	9	67	2.5
k_cat μmole min⁻¹ mg⁻¹	48	23	5.7
k_cat/Kb, min⁻¹	218	53.5	28.5

Kinetic constants were determined at 40°C in 150 mM Tris-HCl buffer (pH 9.0) by varying the substrate and cofactor concentrations in initial velocity studies as described in Materials and Methods. K_a and K_b are the Michaelis constants for NADP⁺ and 2-propanol, respectively. K_ia is the dissociation constant for NADP⁺; k_cat is the turnover number for 2-propanol oxidation. Errors for fitted parameters were in the range of 5% to 10%.