TABLE 1.
Kinetic parameters of sGC activity and inhibition by ATP depending on NO state of the enzyme
| NO state |
kcat |
Ks, WT |
Kic |
Kia |
|||
|---|---|---|---|---|---|---|---|
| WT | DM | WT | DM | WT | DM | ||
| s−1 | μm | mm | mm | ||||
| Basal | 0.029 ± 0.001 | 0.073 ± 0.003 | 70 ± 14 | 0.08 ± 0.02 | 0.06 ± 0.02 | 0.46 ± 0.11 | 0.51 ± 0.17 |
| 1-NO | 1.9a ± 0.1 | 2.8a ± 0.2 | 80 ± 20 | 0.18 ± 0.07 | 0.19 ± 0.07 | 0.43 ± 0.1 | 0.44 ± 0.1 |
| xsNO | 15.0 ± 0.6 | 11.0 ± 0.5 | 30 ± 10 | 0.18 ± 0.07 | 0.30 ± 0.09 | 0.49 ± 0.08 | 1.40 ± 0.27 |
a In the 1-NO state, kcat values were determined based on the concentration of 5c NO complex estimated by deconvolution of final spectra as shown in Fig. 3A.