[4] Certain types of the lipoxygenases, e.g. human and murine 15-lipoxygenase 1, 12-lipoxygenase B, and ALOXE3, are capable of metabolizing fatty acid substrates that are constituents of phospholipids, cholesterol esters, or complex lipids of the skin.

[3][4][5] Lipoxygenases depend on the availability of their polyunsaturated fatty acid substrates which, particularly in mammalian cells, is normally maintained at extremely low levels.

In general, various phospholipase A2s and diacylglycerol lipases are activated during cell stimulation, proceed to release these fatty acids from their storage sites, and thereby are key regulators in the formation of lipoxygenase-dependent metabolites.

[9] Plant lipoxygenase in conjunction with hydroperoxide lyases are responsible for many fragrances and other signalling compounds.

The active site iron is coordinated by Nε of three conserved His residues and one oxygen of the C-terminal carboxyl group.

In addition, in soybean enzymes the side chain oxygen of asparagine is weakly associated with the iron.

Details about the active site feature of lipoxygenase were revealed in the structure of porcine leukocyte 12-lipoxygenase catalytic domain complex[23][25] In the 3D structure, the substrate analog inhibitor occupied a U-shaped channel open adjacent to the iron site.

This channel could accommodate arachidonic acid without much computation, defining the substrate binding details for the lipoxygenase reaction.

Soybean Lipoxygenase 1 exhibits the largest H/D kinetic isotope effect (KIE) on kcat (kH/kD) (81 near room temperature) so far reported for a biological system.

[26] Because of the large magnitude of the KIE, Soybean Lipoxygenase 1 has served as the prototype for enzyme-catalyzed hydrogen-tunneling reactions.