TABLE 3.
Specific enzyme activity and kinetic parameters of the recombinant LysA proteins (DAP decarboxylases) for DAP
| Strain | Sp act (U mg−1) | Km (mM)a | kcat (s−1) | Vmax (U mg−1) |
|---|---|---|---|---|
| A40-4 | 29.87 ± 2.31 | 0.72 ± 0.14 | 41.63 ± 0.88 | 58.28 ± 1.24 |
| A40-3 | 12.68 ± 0.38 | 1.89 ± 0.34 | 26.94 ± 2.42 | 37.71 ± 3.38 |
| B30-1 | 32.77 ± 0.62 | 1.17 ± 0.34 | 40.33 ± 3.73 | 46.79 ± 4.33 |
| B31-7 | 15.34 ± 0.73 | 0.99 ± 0.24 | 13.38 ± 2.49 | 18.33 ± 3.41 |
a
Kinetic parameters were calculated by nonlinear regression fitted directly to the Michaelis-Menten equation using Origin8 software. The initial rates were determined with 0 to 12 mM DAP. The nonlinear fit curves for the decarboxylation of DAP by LysA proteins are shown in Fig. S6.