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

• Published in: Biochimica et biophysica acta Vol. 1081; no. 1; pp. 99 - 105
• Main Authors: Cucurou, C., Battioni, J.P., Daniel, R., Mansuy, D.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 04.01.1991; Elsevier
• Subjects: 15-Lipoxygenase; 5-Lipoxygenase; Analytical, structural and metabolic biochemistry; Arachidonate 15-Lipoxygenase - metabolism; Arachidonate 5-Lipoxygenase - metabolism; binding; Biochemistry; Biochemistry, Molecular Biology; Biological and medical sciences; Chromatography, High Pressure Liquid; Electron Spin Resonance Spectroscopy; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Glycine max; Glycine max - enzymology; Hydroperoxyoctadecadienoic acid; hydrophobicity; Kinetics; Life Sciences; lipoxygenase; Oxidation-Reduction; Oxidoreductases; Peroxidase; Peroxidases; Solanum tuberosum; Solanum tuberosum - enzymology; Substrate Specificity; Vitamin E; Vitamin E - analogs & derivatives; Vitamin E - metabolism; Xenobiotic oxidation; Xenobiotic oxidation; DETAPAC, diethylenetriaminepentaacetic acid; 15-Lipoxygenase; BW755C, 3-amino-1-(3-(trifluoromethyl)-phenyl)-2-pyrazoline; 13-HPOD, 13(S)-hydroxyperoxy-9 Z,11 E-octadecadienoic acid; L-1, soybean lipoxygenase-1 or 15-lipoxygenase; 13-HOD, 13(S)-hydroxy-9 Z,11 E-octadecadienoic acid; NDGA, nordihydroguaiaretic acid; Vitamin E; trolox C, 6-hydroxy-2,5,7,8-tetramethyl-chroman-2-carboxylic acid; 9-HPOD, 9(S)-hydroperoxy-10 E,12 Z-octadecadienoic acid; 5-Lipoxygenase; phenidone, 1-phenyl-3-pyrazolidone; Peroxidase; Hydroperoxyoctadecadienoic acid; 5-PLO, potato 5-lipoxygenase; Potato; Enzyme; Isozyme; Substrate specificity; EPR spectrometry; HPLC chromatography; α-Tocopherol; Soybean; Lipoxygenase
• ISSN: 0005-2760; 0006-3002; 1879-145X; 1878-2434
• DOI: 10.1016/0005-2760(91)90256-H

Potato 5-lipoxygenase (5-PLO) catalyzes the reduction of 13(S)-hydroperoxy-9 Z,11 E-octadecadienoic acid (13-HPOD) in the presence of vitamin E. 1 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.