Table 1.
Parameters of Michaelis-Menten kinetics and results of computational binding.
| Temperature (℃) | Michaelis-Menten Kinetics | Energy Constant | Computational Docking | ||||
|---|---|---|---|---|---|---|---|
|
Km (mM) |
Vmax (mM/min) |
Adj. R2 |
ΔGd (kJ/mol) |
Correctly Docked L-DOPA |
Binding Energy (kJ/mol) |
Binding Affinity, Kd (mM) |
|
| 25 | 0.41 ± 0.11 | 0.029 ± 0.003 | 0.95 | −11.57 ± 2.97 | 005 | 25.71 | 0.032 |
| 31 | 0.52 ± 0.31 | 0.032 ± 0.007 | 0.83 | −12.74 ± 2.90 | 002 | 26.75 | 0.011 |
| 37 | 0.70 ± 0.25 | 0.038 ± 0.005 | 0.94 | −13.32 ± 2.87 | 002 009 |
26.71 25.21 |
0.019 |
| 43 | 0.62 ± 0.15 | 0.057 ± 0.003 | 0.96 | −13.90 ± 2.83 | 003 | 26.00 | 0.016 |
Note: Correctly docked L-DOPA assumes the pose of L-DOPA molecule located in the tyrosinase active site.