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. 2022 Jul 19;298(9):102282. doi: 10.1016/j.jbc.2022.102282

Table 1.

Kinetic parameters of open and closed mutants

Enzyme Khalf (μM) kcat (s−1) Vmax (nM/s) kcat/Khalf (s−1 μM−1) h R (2)
Stable-5-LOX 19.0 ± 0.8 0.43 ± 0.02 108 ± 6 0.023 ± 0.001 2.11 ± 0.07 0.997 ± 0.0003
N-Elongated 6.2 ± 0.2 1.67 ± 0.005 417 ± 1 0.27 ± 0.01 2.76 ± 0.08 0.988 ± 0.008
Uncorked 9.6 ± 0.7 0.35 ± 0.01 87 ± 3 0.036 ± 0.001 2.13 ± 0.03 0.995 ± 0.003
N-Elongated-Uncorked 9 ± 1.0 1.62 ± 0.09 400 ± 20 0.18 ± 0.02 2.3 ± 0.3 0.98 ± 0.01
C-Unlocked 13.0 ± 0.9 0.31 ± 0.01 77 ± 3 0.024 ± 0.001 3.0 ± 0.9 0.97 ± 0.02
C-Locked-Open 4.6 ± 0.1 0.28 ± 0.001 71 ± 0.3 0.062 ± 0.002 2.55 ± 0.01 0.997 ± 0.0008
C-Locked-Closed 15.3 ± 0.8 0.46 ± 0.01 114 ± 3 0.030 ± 0.002 1.80 ± 0.09 0.994 ± 0.002
Penta-5-LOX 4.5 ± 0.2 1.67 ± 0.03 418 ± 6 0.37 ± 0.01 3.0 ± 0.2 0.95 ± 0.01
Stable-5-LOX + 13-Hpode 7.7 ± 0.1 0.15 ± 0.0008 37 ± 0.2 0.02 ± 0.0003 1.95 ± 0.03 0.9979 ± 0.0006

All measurements were completed in triplicate with error shown as SD. Data were fit to the Hill equation, which generates Khalf rather than KM. R2 refers to the corresponding goodness of fit.