Table 2.
Comparison of catalytic properties of HadX with other flavin reductases
| Enzyme | Organism | Cofactor | Oxygenase partner | Kinetic parameters |
CT complex formation | Ref. | ||||
|---|---|---|---|---|---|---|---|---|---|---|
| kred | kox with O2 | KD, flox | KD, flred | k, flred transfer | ||||||
| s−1 | m−1 s−1 | μm | s−1 | |||||||
| HadX | R. pickettii | FAD bound | HadA | 104 ± 1 | 4.3 ± 0.1 × 103 | 0.38 ± 0.02 | 1.7 ± 0.6 | 7.0 ± 0.6 | Yes | This study |
| TcpX | R. eutropha | FAD | TcpA | –a | – | – | – | – | – | 29 |
| TftD | B. cepacia | FAD | TftD | – | – | 1.8 ± 0.1 | – | – | – | 9, 30 |
| C1 (C1–HPA) | A. baumannii | FMN bound | C2 | 11.6 ± 0.3 (300) | 820 (820) | 0.006 ± 0.001 (0.038 ± 0.007) | – (≫0.038 ± 0.007) | ∼0.35 (∼80) | Yes | 19–21, 44, 46 |
| ActVB | S. coelicolor | FMN bound | ActVA | – | – | 4.4 ± 0.6 | 6.6 ± 0.6 | 5.0 ± 0.4 | Yes | 31, 34, 35 |
| LuxG | P. leiognathi TH1 | FMN | LuxAB | 68 ± 6 | – | Not bind | – | ∼5.0 | Yes | 36–38 |
| HpaC | E. coli | FAD | HpaB | – | – | 5.8 ± 0.3 | – | – | – | 65 |
| PheA2 | B. thermoglucosidasius A7 | FAD bound | PheA1 | – | – | Tight | – | – | – | 66 |
| StyB | Pseudomanas sp. | FAD | StyA | – | – | 2.3 ± 0.3 | – | – | – | 67 |
a Dash (–) indicates none reported.