TABLE 4.
Kinetic parameters of the wild-type and mutant ColH enzymesa
| Enzyme | Km (mM) | kcat (s−1) | kcat / Km (mM−1 s−1) |
|---|---|---|---|
| Wild type | 0.88 ± 0.21 | 0.11 ± 0.019 | 0.13 |
| E446A | 0.88 ± 0.13 | 0.026 ± 0.0039 | 0.030 |
| E447Q | 0.65 ± 0.10 | 0.0055 ± 0.00054 | 0.0085 |
| E451A | 0.80 ± 0.39 | 0.0072 ± 0.0024 | 0.0090 |
a
The activities of the wild-type and mutant ColH enzymes were determined by using Pz peptide as a substrate. Km and kcat values were obtained by Lineweaver-Burk plot analysis. Values are means ± standard deviations of triplicate measurements.