Table 1. Characterization of Michaelis–Menten Kinetics of Top Variants.
| variant | Kma (μM) | kcata (s–1) | kcat/Km (mM–1 s–1) | Kdb (μM) |
|---|---|---|---|---|
| CHMOAcineto | 6.7 ± 2.0 | 15.0 ± 1.3 | 2200 | 1.60 ± 0.06 |
| L1-1 | 3.5 ± 0.3 | 24.2 ± 1.4 | 7058 | 0.19 ± 0.07 |
| L3-4 | 5.0 ± 1.5 | 16.3 ± 1.8 | 3187 | 0.14 ± 0.02 |
a
Catalytic rates were obtained via incubation of the isolated enzyme with varying amounts of substrate, and kinetic parameters (Km, kcat) were determined by fitting to the Michaelis–Menten equation.
b
The Kd value was determined by fitting the data of catalytic activity of the holoenzyme versus concentration of FAD.