Table 1.
Kinetic Parameters for the Reduction of Different Substrates with saFabI
| Substrates |
kcat
(min−1) |
Km
(μM) |
kcat/Km
(min−1 μM−1) |
|---|---|---|---|
| Crotonyl NACa | 1.5 ± 0.5 | 8.0 ± 0.3 | 0.20 ± 0.06 |
| Crotonyl CoAb,c | - | - | - |
| Crotonyl saACPc | 11.6 ± 1.1 | 11.5 ± 2.0 | 1.1 ± 0.2 |
| Dodecenoyl NACc | 30.4 ± 1.6 | 23.3 ± 2.9 | 1.3 ± 0.2 |
| Dodocenoyl CoA c | 18.0 ± 0.8 | 24.1 ± 2.5 | 0.8 ± 0.1 |
| Dodecenoyl saACP d | 130.2 ± 9.1 | 4.5 ± 0.5 | 29.5 ± 5.0 |
| NADHe | - | - | 0.010 ± 0.001 |
| NADPH d,e | 130.2 ± 9.1 | 70.8 ± 6.0 | 1.840 ± 0.311 |
a
Parameters were measured by Heath et al. (20);
b
no enzymatic activity was observed;
c
reactions were carried out with 300 μM NADPH;
d
Km and kcat values were obtained by fitting data into the sequential mechanism equation;
e
reactions were carried out with 20 μM DDsaACP.