Table 1.
Steady-state kinetic parameters for DSA and ESA hydrolysis by MccF wild-type and mutant enzymes
| Km, μM | kcat, s-1 | kcat/Km, M-1 s-1 | Relative kcat/Km* | |
| DSA | ||||
| Wild type | 74.31 | 6.96 | 9.37E4 | 1.000 |
| N220A | 186.32 | 2.22 | 1.19E4 | 0.126 |
| K247A | 133.92 | 3.27 | 2.44E4 | 0.260 |
| S118A | ND | ND | ||
| ESA | ||||
| Wild type | 51.64 | 0.58 | 1.13E4 | 1.000 |
| W186F | 218.77 | 0.39 | 1.78E3 | 0.157 |
| W186A | ND | ND | ||
| R246A | 154.27 | 0.56 | 3.64E3 | 0.322 |
| N220A | 105.89 | 0.62 | 5.85E3 | 0.518 |
| K247A | 238.92 | 0.08 | 3.51E2 | 0.031 |
| N220A/K247A | ND | ND | ||
ND, no detectable activity precluded kinetic parameter determination.
*The kcat/Km of mutant enzyme relative to wild-type enzyme.