99%-pure 3-oxalinolenic acid in 10-15% overall yield. 3-Oxalinolenic acid was efficiently oxygenated by soybean lipoxygenase-1 into 3-oxa-13(S)-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid, and this hydroperoxide could be further converted chemically into 3-oxa-13(S)-hydroxy-9(Z),11 (E),15(Z)-octadecatrienoic acid and 3-oxa-13-oxo-9(Z),11 (E),15(Z)-octadecatrienoic acid. The 3-oxa-hydroperoxide also served as the substrate for the plant enzymes allene oxide synthase, divinyl ether synthase, and hydroperoxide lyase to produce 3-oxa-12-oxo-10,15(Z)-phytodienoic acid and other 3-oxa-oxylipins that were characterized by MS. 3-Oxalinolenic acid was not oxygenated by 9-lipoxygenase from tomato but was converted at a slow rate into 3-oxa-9(S)-hydroperoxy-10(E),12(Z),15(Z)-octadecatrienoic acid by recombinant maize 9-lipoxygenase. Recombinant alpha-dioxygenase-1 from Arabidopsis thaliana catalyzed the conversion of 3-oxalinolenic acid into a 2-hydroperoxide, which underwent spontaneous degradation into a mixture of 6,9,12-pentadecatrienol and 6,9,12-pentadecatrienyl formate. A novel alpha-dioxygenase from the moss Physcomitrella patens was cloned and expressed and was found to display the same activity with 3-oxalinolenic acid as Arabidopsis thaliana alpha-dioxygenase-1. Lipoxygenase-generated 3-oxa-oxylipins are resistant toward beta-oxidation and have the potential for displaying enhanced biological activity in situations where activity is limited by metabolic degradation.