Peroxidase-like activity of lipoxygenases: different substrate specificity of potato 5-lipoxygenase and soybean 15-lipoxygenase and particular affinity of vitamin E derivatives for the 5-lipoxygenase.
Potato 5-lipoxygenase (5-PLO) catalyzes the reduction of 13(S)-hydroperoxy-9Z,11E-octadecadienoic acid (13-HPOD) in the presence of vitamin E. I mol of vitamin E is required to consume 2 mol of 13-HPOD. The mechanism of the 5-PLO-catalyzed oxidation of vitamin E by 13-HPOD is similar to that previously established for the soybean 15-lipoxygenase (L-1)-catalyzed oxidation of phenidone by 13-HPOD, and seems to involve a one-electron reduction of the O-O bond of 13-HPOD. 5-PLO and L-1 exhibit very different substrate specificities and pH profiles for their peroxidase-like activity. Actually, among the 20 compounds containing various reducible functions and the 10 derivatives of vitamin E which have been studied, only four products containing hydrophobic long chains, ascorbic acid 6-palmitate, the trolox esters of octanol and undecanol, and vitamin E exhibit high peroxidase-like activities for 5-PLO. On the contrary, much more compounds, even not very hydrophobic, are good substrates for the peroxidase-like activity of L-1.
Cucurou
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Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques (URA 400 CNRS), Université René Descartes, Paris France.
Battioni
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JP
Daniel
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R
Mansuy
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D
D001093:Arachidonate 15-Lipoxygenase / Q000378:metabolism*; D001094:Arachidonate 5-Lipoxygenase / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004578:Electron Spin Resonance Spectroscopy; D007700:Kinetics; D010084:Oxidation-Reduction; D010544:Peroxidases; D011198:Solanum tuberosum / Q000201:enzymology*; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity; D014810:Vitamin E / Q000031:analogs & derivatives* / Q000378:metabolism*
D014810:Vitamin E; D010544:Peroxidases; D001093:Arachidonate 15-Lipoxygenase; D001094:Arachidonate 5-Lipoxygenase