TABLE 6.
Kinetic parameters of bacterial IMPDHs and their ΔCBS constructs
| Enzyme | kcat | IMP, Km | NAD+, Km | NAD+ Kii |
|---|---|---|---|---|
| s−1 | μm | μm | mm | |
| BaIMPDH | 5.3 ± 0.1 | 64 ± 16 | 550 ± 100 | 3.9 ± 0.8 |
| BaIMPDHΔS | 6.1 ± 0.3 | 61 ± 4 | 560 ± 50 | 5.3 ± 0.7 |
| BaIMPDHΔL | 4.5 ± 0.2 | 150 ± 20 | 460 ± 50 | 3.8 ± 0.5 |
| CjIMPDH | 2.2 ± 0.1 | 55 ± 5 | 220 ± 30 | 20 ± 2 |
| CjIMPDHΔS | 1.9 ± 0.1 | 27 ± 3 | 520 ± 70 | 6.4 ± 0.7 |
| ClpIMPDH | 2.9 ± 0.2 | 100 ± 10 | 370 ± 40 | 13 ± 2 |
| ClpIMPDHΔL | 1.8 ± 0.1 | 49 ± 4 | 510 ± 60 | 9 ± 1 |
| VcIMPDHa | 2.1 ± 0.2 | 80 ± 10 | 1200 ± 200 | NDb † |
| VcIMPDHΔL | 5.2 ± 0.3 | 87 ± 13 | 1100 ± 100 | 13 ± 3 |
a Data are from Ref. 11.
b ND means not determined.