Oxidation of dilinoleoyl phosphatidylcholine by lipoxygenase 1 from soybeans.
Soybean lipoxygenase-1 is able to oxidize dilinoleoyl phosphatidylcholine at pH 7.5 and 10. The reaction could be followed spectrophotometrically from the increase of the absorbance at 234 nm. An intermediate product and a final product were detected. In the intermediate product only one of the linoleoyl chains (either sn1 or sn2) was oxidized. In the final product, both linoleic acid units were converted into hydroperoxides. Apparently, oxidation of one of the linoleoyl chains leads to a disruption of the structure of the mixed bilayer disk, making the remaining fatty acid unit more accessible to the action of the enzyme. The specificity of lipoxygenase-1 when acting on phospholipids is not affected by pH. The exclusive production of 13-hydroperoxyoctadecadienoic acid derivatives of dilinoleoyl phosphatidylcholine at pH 7.5 and 10 may result from the blockage of the carboxylic end of the fatty acid.
Pérez-Gilabert
M
M
Bijvoet Center for Biomolecular Research, Department of Bio-organic Chemistry, Utrecht University, The Netherlands.
Veldink
G A
GA
Vliegenthart
J F
JF
D008401:Gas Chromatography-Mass Spectrometry; D008084:Lipoxygenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010713:Phosphatidylcholines / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity
D010713:Phosphatidylcholines; C002448:1,2-linoleoylphosphatidylcholine; D008084:Lipoxygenase; D010741:Phospholipases A