Table 3. Kinetic properties of native (nLcc4) and Endo H-deglycosylated lcc4 (dLcc4) a .
Protein | Substrate | Specific activity (U/mg) b | k cat (s −1) | K m (μM) | k cat/K m (s −1μM−1) | Optimal reaction conditions (°C/pH) |
---|---|---|---|---|---|---|
nLcc4 | ABTS | 2996 | 3382 | 65.0±6.5 | 52 | 70/2.5 |
dLcc4 | ABTS | 2342 | 2488 | 48.3±5.5 | 52 | 70/2.5 |
nLcc4 | 2,6-DMP | 119 | 134 | 412.1±28.0 | 0.33 | 60/3.5 |
dLcc4 | 2,6-DMP | 114 | 121 | 437.1±23.9 | 0.28 | 60/3.5 |
a The enzymatic reaction was performed at the respective optimal temperatures and pHs as indicated.
b One unit of enzyme activity was defined as the amount of enzyme that oxidizes 1 μmol of substrate per minute under optimal reaction conditions.