Table 2.
Dalziel steady-state kinetic parameters of native and refolded G6PD.
| Native G6PD | Refolded G6PD | |
| Specific activity (IU/mg) | 180 ± 10 | 175 ± 12 |
| ϕo(s) | 0.00366 ± 0.00023 | 0.00358 ± 0.00031 |
| ϕNADP+(μMs) | 0.0259 ± 0.0041 | 0.0249 ± 0.0037 |
| ϕG6P(μMs) | 0.191 ± 0.021 | 0.196 ± 0.026 |
| ϕNADP+G6P(μM2s) | 1.61 ± 0.22 | 1.55 ± 0.18 |
| ϕNADP+G6P/ϕNADP+(μM) | 57.98 ± 0.68 | 62.6 ± 3.4 |
| ϕNADP+G6P/ϕG6P(μM) | 7.77 ± 0.68 | 7.90 ± 0.37 |
| kcat(s-1) | 275 ± 18 | 279 ± 6.8 |
| KmNADP+(μM) | 7.07 ± 1.13 | 6.94 ± 0.34 |
| KmG6P(μM) | 52 ± 4 | 54.7 ± 3.2 |
| kcat/KmNADP+(μM-1 s-1) | 39.7 ± 7.5 | 40.3 ± 2.5 |
| kcat/KmG6P(μM-1 s-1) | 5.31 ± 0.69 | 5.1 ± 0.34 |
The table shows the four constants of the reciprocal initial-rate equation [26] as estimated for wild-type G6PD and refolded enzyme. The corresponding of kcat values and the true Km values for both substrates are also listed. The parameters in each case were obtained from three independent experiments.