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Steady state kinetics and product profile of wt-hALOX12 and its two 414 mutants with mead acid to examine the interacting double bond of the substrate with F414.
| Enzymes | KM (µM) | kcat (s−1) | kcat/KM (µM)−1s−1 | Products (%) | |
|---|---|---|---|---|---|
| 12-HETE | 15-HETE | ||||
| Wt-hALOX12 | 1.3 ± 0.09 | 1.5 ± 0.03 | 1.2 ± 0.06 | 100 ± 5 | 0 |
| F414L | 1.8 ± 0.5 | 0.60 ± 0.05 | 0.33 ± 0.07 | 100 ± 5 | 0 |
| F414W | 1.9 ± 0.2 | 8.5 ± 0.2 | 4.5 ± 0.3 | 100 ± 5 | 0 |
