Table I.
Kinetic Studies of the Different Hybrid β-Lactamases
| BlaP (SmaI) | BlaPChBDI | BlaPChBDII | BlaPChBDIII | |
|---|---|---|---|---|
| KM (μM) | 40 ± 2 | 20 ± 1 | 41 ± 1 | 56 ± 2 |
| kcat (s−1) | 490 ± 20 | 195 ± 5 | 340 ± 10 | 415 ± 7 |
| kcat/KM (μM−1 s−1) | 12.2 ± 0.8 | 9.7 ± 0.5 | 8.3 ± 0.3 | 7.4 ± 0.3 |
The substrate was 100 μM nitrocefin. The values are compared with those reported for the parental enzyme without any insert (BlaP SmaI).27 Each kinetic has been performed twice in triplicates. These values represent the averages ± SD of the two independent experiments.