Natural polyamines inhibit soybean (Glycine max) lipoxygenase-1, but not the lipoxygenase-2 isozyme.
Natural polyamines are shown to inhibit dioxygenase activity of soybean lipoxygenase-1, but they were ineffective toward the lipoxygenase-2 isozyme. The inhibitory power was dependent on the number of basic groups in the molecule, in the order spermine > spermidine > cadaverine >/= putrescine. Both spermidine and spermine acted as uncompetitive inhibitors of lipoxygenase-1 with respect to linoleic acid, the inhibition constants being 2.70 and 0.80 mM, respectively. The inhibitory power apparently correlated with the radical-trapping ability of the polyamines. Spermidine and spermine also inhibited the co-oxidase and peroxidase activities of lipoxygenase-1 and were effective inhibitors of lipoxygenase activity in lentil root protoplasts.
Department of Experimental Medicine and Biochemical Sciences, University of Rome "Tor Vergata," Via di Tor Vergata 135, Rome, I-00133, Italy.
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Maccarrone
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Baroni
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Finazzi-Agrò
D004305:Dose-Response Relationship, Drug; D007887:Fabaceae / Q000201:enzymology; D007424:Intracellular Fluid / Q000201:enzymology; D007527:Isoenzymes / Q000037:antagonists & inhibitors*; D015227:Lipid Peroxidation / Q000187:drug effects; D008084:Lipoxygenase / Q000187:drug effects / Q000378:metabolism*; D016859:Lipoxygenase Inhibitors / Q000494:pharmacology*; D018517:Plant Roots / Q000201:enzymology; D010946:Plants, Medicinal; D011073:Polyamines / Q000494:pharmacology*; D011523:Protoplasts / Q000201:enzymology; D013025:Glycine max / Q000201:enzymology*
D007527:Isoenzymes; D016859:Lipoxygenase Inhibitors; D011073:Polyamines; D008084:Lipoxygenase