Table 2.
Activity of cascade enzymes depending on the ammonium source. Reactions were carried out in triplicates at 50 °C containing 100 mM HEPES pH 7.35 and either 5 mM NAD or 0.4 mM NADH and a final concentration of 200 mM ammonium (except H2O control). For BsGDH 100 mM glucose, for PtKDGA 1 mM KDG and an excess of MjALDH, for CcDHAD 20 mM gluconate and excess of PtKDGA/ MjALDH and for AfAlaDH 1 mM pyruvate were used. Average values are given in U/mL ± standard deviation.
| [U/mL] | BsGDH | CcDHAD | PtKDGA | AfAlaDH |
|---|---|---|---|---|
| H2O | (4.4 ± 0.1)*103 | 12.3 ± 1.6 | 41.6 ± 1.3 | 2.9 ± 1.5 |
| NH4Cl | (5.8 ± 0.7)*103 | 0 | 21.4 ± 2.8 | 91.0 ± 0.2 |
| NH4NO3 | (5.7 ± 0.1)*103 | 0 | 4.8 ± 0.4 | 77.8 ± 1.0 |
| (NH4)2HPO4 | (5.0 ± 0.3)*103 | 2.5 ± 0.4 | 31.5 ± 2.8 | 77.5 ± 3.1 |
| (NH4)2SO4 | (5.0 ± 0.1)*103 | 8.3 ± 0.5 | 31.5 ± 0.2 | 86.2 ± 4.3 |