TABLE 4.
Apparent Michaelis-Menten constants (Km) and catalytic constants (kcat) of AaP II for veratryl alcohol, benzyl alcohol, ABTS, and DMPa
Substrate | pH | Km (μM) | kcat (s−1) | kcat/Km (M−1 s−1) |
---|---|---|---|---|
Veratryl alcohol | 7 | 2,367 | 85 | 3.58 × 104 |
Benzyl alcohol | 7 | 1,001 | 269 | 2.69 × 105 |
ABTS | 4.5 | 37 | 283 | 7.67 × 106 |
DMP | 7 | 298 | 108 | 3.61 × 105 |
H2O2 | 7 | 1,313 | 367 | 2.79 × 105 |
Reactions were performed in sodium phosphate/citrate buffer (pH 7 or 4.5) in the presence of 2 mM H2O2. The Km for H2O2 was determined in the presence of 5 mM benzyl alcohol. The values are means for three parallel experiments, and the standard deviations were <5%.