Enzyme | Substrate | Km (mM) | kcat (min−1) | kcat/Km (mM−1 min−1) |
---|
F-BbAmDH | NADH | 0.16 ± 0.02 | 0.65 ± 0.01 | 4.03 |
L-BcAmDH | NADH | 0.021 ± 0.004 | 1.09 ± 0.1 | 51.40 |
L-EsAmDH | NADH | 0.052 ± 0.005 | 1.62 ± 0.22 | 31.15 |
- Determination of coenzyme kinetic parameters using the same substrate 2-pentanone. The values were generated by fitting the initial specific activity data to the Michaelis–Menten equation using nonlinear regression with GraphPad Prism software. Value is means ± standard deviations. All reactions involved in the kinetic constant calculations were analyzed using a 2 M NH4Cl/NH4OH buffer at optimum pH and temperature. All experiments were repeated 3 times