TABLE 3.
Activity of TbNTR toward different nitrobenzylphosphoramide mustardsa
| Substrate | Mean Km (μM) ± SD | Mean Vmax (nmol NADH oxidized min−1 mg−1) ± SD | Kcat/Km (M−1 s−1) |
|---|---|---|---|
| Nifurtimox | 53.1 ± 15.2 | 423.3 ± 45 | 3.4 × 103 |
| LH7 | 80.3 ± 24.5 | 245.0 ± 34.5 | 1.3 × 103 |
| LH32 | 6.9 ± 0.5 | 832 ± 9 | 5.2 × 104 |
| LH33 | 2.4 ± 0.3 | 654 ± 14 | 1.2 × 105 |
| LH34 | 8.4 ± 0.6 | 706 ± 27 | 4.3 × 104 |
| LH37 | 2.8 ± 0.4 | 1238 ± 48 | 1.8 × 105 |
a
The enzyme activity (Vmax) was calculated using an ε value of 6.22 mM−1. Kcat assumes one catalytic site per 30-kDa monomer.