TABLE 2.
Kinetic parameters of HQD for 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS)a
| No. | Name | Purity (%) | Sp act (U/mg) | kcat (s−1) | Km (μM) | kcat/Km |
|---|---|---|---|---|---|---|
| 03 | AqdC | 100 | 60.2 ± 2.2 | 41.9 ± 1.1b | 5.8 ± 0.4b | 7.3 ± 0.6b |
| 04 | AqdC1 | 98.4 | 20.7 ± 1.2 | 16.0 ± 0.8 | 7.0 ± 0.2 | 2.3 ± 0.2 |
| 06 | HQDN.c. | 100 | 33.6 ± 2.3 | 22.1 ± 0.7 | 4.9 ± 0.4 | 4.6 ± 0.6 |
| 07 | HQDN.f. | 100 | 73.2 ± 2.8 | 43.9 ± 1.5 | 3.1 ± 0.4 | 14.1 ± 1.8 |
| 08 | HQDS.b. | 99.2 | 34.1 ± 2.3 | 27.4 ± 2.3 | 2.7 ± 0.9 | 9.3 ± 1.1 |
| 13 | HQDC.i. | 82.4 | 20.0 ± 3.2 | 15.2 ± 0.9 | 7.3 ± 1.1 | 2.1 ± 0.4 |
| 14 | HQDF.o. | 79.5 | 8.5 ± 1.8 | 7.6 ± 0.4 | 5.0 ± 0.7 | 1.6 ± 0.3 |
Results are represented as means ± standard deviations (from ≥2 biological and 3 technical replicates each). The purity of the protein preparations was determined by densitometric analysis of SDS gels (Fig. S4).
Data from reference 33.