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

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© 2022 The Authors

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

PMC Copyright notice

Kinetic characteristics of open and closed mutants.A and B, saturation curves for Hα2 5-LOX mutants. Triplicate measurements were fit to the Hill equation. A, amino-terminal Hα2 mutants compared to Stable-5-LOX. B, carboxy-terminal Hα2 mutants compared to Stable-5-LOX. C and D, LT production by Stable-5-LOX and N-Elongated-Uncorked. Absorbance at 235 nm and 270 nm versus time records HPETE and LT products, respectively. Duplicate measurements are shown for each with enzyme concentrations of 250 nM and substrate concentrations of 6.3 μM. A saturation curve of LT production by N-Elongated-Uncorked produced by triplicate measurements is shown embedded in panel (D). 5-LOX, 5-lipoxygenase; Hα2, helix-α2; HPETE, hydroperoxyeicosatetraenoic acid.