Table 2.
Kinetic parameters of free enzymes and fusion enzymes
| Enzymes | K m (µM) | V max (µM/min) | K cat (sec−1) | K cat /K m (×106 M−1S−1) |
|---|---|---|---|---|
| For IPP | ||||
| FPPS+ECS | 5.64 ± 0.2 | 0.81 ± 0.1 | 1.4 ± 0.1 | 0.24 ± 0.1 |
| FPPS‐ECS Fusion | 4.71 ± 0.1 | 0.92 ± 0.1 | 1.88 ± 0.1 | 0.40 ± 0.1 |
| For DMAPP | ||||
| FPPS+ECS | 2.82 ± 0.2 | 0.81 ± 0.1 | 1.4 ± 0.1 | 0.49 ± 0.1 |
| FPPS‐ECS Fusion | 2.35 ± 0.1 | 0.92 ± 0.1 | 1.88 ± 0.1 | 0.80 ± 0.1 |
| For FPP | ||||
| ECS | 3.74 ± 0.2 | 1.23 ± 0.1 | 0.95 ± 0.1 | 0.25 ± 0.1 |
Reaction conditions: 1.5 nM of free enzymes (added together) and fusion enzymes were used for the measurement of kinetic parameters against IPP. The reaction was performed as described in the method section using 1–30 µM IPP and 0.5‐15 µM dimethylallyl pyrophosphate respectively. For ECS, FPP was used as a substrate
ECS, epi‐cedrol synthase; FPP, farnesyl diphosphate; FPPS, farnesyl pyrophosphate synthase; IPP, isopentyl diphosphate.