Lipoxygenase-1 (LOX-1 (used in plant biology, specifically for soybean enzyme soybean lipoxygenase-1 is abbreviated SLO-1 in some literature))

Lipoxygenase-1 (commonly abbreviated LOX-1 or SLO-1 in soybean) is a member of the large **lipoxygenase** family of non-heme iron-containing enzymes that catalyze the regio- and stereo-selective dioxygenation of polyunsaturated fatty acids (PUFAs) to form fatty acid hydroperoxides[1][3][7]. The canonical Lipoxygenase-1—first isolated and structurally characterized in soybean—is a prototype plant enzyme containing an amino-terminal PLAT domain and a large C-terminal catalytic domain with an iron center buried in a helical core[1][2][5]. Lipoxygenase-1 has been studied as a model for understanding enzyme-catalyzed hydrogen transfer (notably with large kinetic isotope effects due to quantum tunneling), substrate selectivity, and protein structural dynamics[5][1]. Functionally, it initiates the peroxidation of free or esterified fatty acids, controlling multiple biological pathways such as plant development and defense, while in mammalian systems, homologous enzymes generate key inflammation mediators[6][3][7]. It is a well-established **therapeutic target** in disorders involving oxidative stress and inflammation, though most drug efforts focus on human isoforms such as 5-lipoxygenase and 15-lipoxygenase rather than SLO-1 itself.

Other names

soybean lipoxygenase-1SLO-1LOX-1linoleate:oxygen oxidoreductaseEC 1.13.11.12

Inhibition of hydroperoxidation of fatty acids Blockage of biosynthesis of eicosanoid precursors (in animal systems) Redox catalysis inhibition at the non-heme iron site