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

Table 1.

Kinetic constants for mutant enzymes

Kinetic constants Wild-type E60A E60D
Ka, μM 83 140 11
Kb, mM 0.22 0.43 0.20
Kia, μM 9 67 2.5
kcat μmole min−1 mg−1 48 23 5.7
kcat/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. Ka and Kb are the Michaelis constants for NADP+ and 2-propanol, respectively. Kia is the dissociation constant for NADP+; kcat is the turnover number for 2-propanol oxidation. Errors for fitted parameters were in the range of 5% to 10%.