etheroleic-acid and colneleic-acid

Treatment of the first leaves of barley seedlings with the oxylipin colneleic acid, or the two trihydroxy oxylipins 9,12,13-trihydroxy-11(E)-octadecenoic acid and 9,12,13-trihydroxy-10(E)-octadecenoic acid, reduced infection of that leaf by the powdery mildew fungus Blumeria graminis Speer f sp hordei Marchal. When applied to first leaves, etheroleic acid and colneleic acid, as well as the trihydroxy oxylipin 9,12,13-trihydroxy-10(E),15(Z)-octadecadienoic acid, also reduced mildew infection in second leaves. In all cases where local and systemic effects against mildew were observed, activity of the defence-related enzyme phenylalanine ammonia lyase (PAL) was increased, but only following challenge inoculation with powdery mildew. Peroxidase activity was not affected by oxylipin treatment or mildew inoculation. Whether the effects observed were due to the oxylipins or to breakdown products is not known, since no information is available on the stability of these particular oxylipins on leaf surfaces. Nevertheless, these data represent the first report of systemic effects against pathogen infection following pre-treatment with oxylipins.

Topics: Ascomycota; Fatty Acids, Unsaturated; Fungicides, Industrial; Hordeum; Plant Leaves

[1-14C]alpha-Linolenic acid was incubated with a particulate fraction of homogenate of leaves of the meadow buttercup (Ranunculus acris L.). The main product was a divinyl ether fatty acid, which was identified as 12-[1'(Z),3'(Z)-hexadienyloxy]-9(Z),11(E)-dodecadienoic acid. Addition of glutathione peroxidase and reduced glutathione to incubations of alpha-linolenic acid almost completely suppressed formation of the divinyl ether acid and resulted in the appearance of 13(S)-hydroxy-9(Z), 11(E),15(Z)-octadecatrienoic acid as the main product. This result, together with the finding that 13(S)-hydroperoxy-9(Z), 11(E),15(Z)-octadecatrienoic acid served as an efficient precursor of the divinyl ether fatty acid, indicated that divinyl ether biosynthesis in leaves of R. acris occurred by a two-step pathway involving an omega6-lipoxygenase and a divinyl ether synthase. Incubations of isomeric hydroperoxides derived from alpha-linolenic and linoleic acids with the enzyme preparation from R. acris showed that 13(S)-hydroperoxy-9(Z),11(E)-octadecadienoic acid was transformed into the divinyl ether 12-[1'(Z)-hexenyloxy]-9(Z), 11(E)-dodecadienoic acid. In contrast, neither the 9(S)-hydroperoxides of linoleic or alpha-linolenic acids nor the 13(R)-hydroperoxide of alpha-linolenic acid served as precursors of divinyl ethers.

Topics: alpha-Linolenic Acid; Chlorophyll; Color; Cytochrome P-450 Enzyme System; Ethers; Fatty Acids, Unsaturated; Lipoxygenase; Magnoliopsida; Oxidation-Reduction; Oxidoreductases; Plant Leaves; Plant Proteins; Vinyl Compounds

The microsomal fraction of homogenate of garlic (Allium sativum L.) bulbs contains a divinyl ether synthase which catalyzes conversion of (9Z,11E,13S)-13-hydroperoxy-9, 11-octadecadienoic acid and (9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatri eno ic acid into (9Z,11E,1'E,)-12-(1'-hexenyloxy)-9,11-dodecadienoic acid (etherolenic acid) and (9Z,11E,1'E,3'Z)-12-(1',3'-hexadienyloxy)-9,11-dode cadienoic acid (etherolenic acid), respectively. Two isomers of etherolenic acid were isolated. As shown by NMR spectrometry, the double bond configurations of these compounds were (9E,11E,1'E) and (9Z,11Z,1'E). Experiments with linoleic acid (13R,S)-hydroperoxide demonstrated that the S enantiomer was a much better substrate for the divinyl ether synthase compared to the R enantiomer. Incubation of (9Z,11E,13S)-[18O2]hydroperoxy-9,11-octadecadienoic acid led to the formation of etherolenic acid which retained 18O in the ether oxygen. An intermediary role of an epoxyallylic cation in etherolenic acid biosynthesis is postulated.

Topics: Chromatography, High Pressure Liquid; Cytochrome P-450 Enzyme System; Fatty Acids, Unsaturated; Garlic; Isomerism; Leukotrienes; Linoleic Acids; Lipid Peroxides; Magnetic Resonance Spectroscopy; Microsomes; Oxidoreductases; Plant Proteins; Plants, Medicinal; Substrate Specificity