Table 1. Enzymatic Activity and Kinetic Parameters of Recombinant ChLAC8 Toward Different Monolignols.
Substrate | Vmax (pKAT mg−1) | Km (μM) | Kcat (s−1) | Kcat/Km (M−1 s−1) |
---|---|---|---|---|
Caffeyl alcohol | 284.4 ± 50.4a | 210.3 ± 90.6a | 0.019 ± 0.003a | 92.53 |
Coniferyl alcohol | N.D. | N.D. | N.D. | N.D. |
Sinapyl alcohol | 192.0 ± 12.8 | 60.2 ± 16.7 | 0.013 ± 0.001 | 218.0 |
Purified recombinant ChLAC8 (10 to 20 μg) was incubated with 25 to 800 μM substrates at 30°C for 30 min. Three enzyme assays were performed at each substrate concentration, and the Vmax and Km values were calculated by nonlinear regression analysis. The significance of difference in kinetic parameters between caffeyl alcohol and sinapyl alcohol was estimated with the unpaired two-tailed Student’s t test, and P-values < 0.05 were deemed significant. N.D., not detected.
Significant difference found.