Table I. Kinetic parameters of recombinant AtPAO5.
kcat and Km values were obtained from the Lineweaver-Burk plot analyses. Experiments were repeated at least three times and the mean ± sd values are displayed. ND, not determined.
| Substrate |
pH 7.5 |
pH 6.5 |
||||
|---|---|---|---|---|---|---|
| kcat | Km | kcat/Km | kcat | Km | kcat/Km | |
| S−1 | μM | M−1 s−1 | S−1 | μM | M−1 s−1 | |
| Spm | 0.069 ± 0.003 | 25.56 ± 2.07 | 2,700 ± 142 | 0.009 ± 0.001 | 78.67 ± 7.13 | 115 ± 18 |
| T-Spm | 0.115 ± 0.007a | 5.09 ± 1.06a | 23,256 ± 3,299a | 0.035 ± 0.003 | 13.65 ± 1.50 | 2,596 ± 68 |
| NorSpm | 0.086 ± 0.006 | 25.54 ± 1.81 | 3,386 ± 111 | 0.012 ± 0.001 | 15.81 ± 0.64 | 747 ± 17 |
| N1-AcSpm | 0.084 ± 0.004a | 1.92 ± 0.16a | 44,020 ± 1,943a | 0.025 ± 0.003a | 2.18 ± 0.57a | 12,323 ± 2,409a |
| Spd | 0.009 ± 0.002 | 68.30 ± 35.61 | 185 ± 98 | ND | ND | ND |
The reaction occurred in a noncanonical Michaelis-Menten fashion. In <10 μm substrate concentration, the reaction occurred linearly. In cases with >20 μm substrate concentration, each reaction was markedly repressed. In those cases, the values were calculated from the data with one-order reaction.