1985
DOI: 10.1016/0006-291x(85)90453-x
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Oxygenation of phosphatidylcholine by human polymorphonuclear leukocyte 15-lipoxygenase

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Cited by 57 publications
(25 citation statements)
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“…On chiral analysis the 9-HANA product chromatographed as one main peak with no definite minor enantiomer, so it was not possible to determine order of elution and infer chirality. We also tested 1-palmitoyl-2-linoleoylphosphatidycholine as a potential substrate for AtLOX1 using the bile salt deoxycholate as detergent, a condition that achieves reaction with plant 13-LOX [26], coral 8R-LOX [9], as well as several mammalian arachidonate 12-LOX and 15-LOX [27][28][29][30]. However, we could detect no reaction with the recombinant 9-LOX, in agreement with a result reported for a purified tomato 9-LOX [20].…”
Section: Catalytic Activity With Other Substratessupporting
confidence: 88%
See 1 more Smart Citation
“…On chiral analysis the 9-HANA product chromatographed as one main peak with no definite minor enantiomer, so it was not possible to determine order of elution and infer chirality. We also tested 1-palmitoyl-2-linoleoylphosphatidycholine as a potential substrate for AtLOX1 using the bile salt deoxycholate as detergent, a condition that achieves reaction with plant 13-LOX [26], coral 8R-LOX [9], as well as several mammalian arachidonate 12-LOX and 15-LOX [27][28][29][30]. However, we could detect no reaction with the recombinant 9-LOX, in agreement with a result reported for a purified tomato 9-LOX [20].…”
Section: Catalytic Activity With Other Substratessupporting
confidence: 88%
“…While caution is warranted in interpretation of negative results, this lack of reaction classifies the linoleate 9-LOX along with other LOX enzymes that are predicted to exhibit carboxyl end-first binding and that show no reaction with very large phospholipid esters (arachidonate 8S-LOX and 5S-LOX) [9,28]. (By contrast, all the LOX enzymes that have predicted tail-first substrate binding do react specifically with phospholipid ester substrates [5,9,[26][27][28][29][30]). Again, our interpretation is that the 9S-LOX active site can accommodate substrates with C-1 appendages of the size of ethanolamide or glycerol, and that overall, the carboxyl end-first binding is the most satisfactory model for oxygenations by linoleate 9S-LOX enzymes.…”
Section: Discussionmentioning
confidence: 99%
“…Docosahexaenoic acid, an ω-3 PUFA is also oxidized by 15-lipoxygenase as part of the synthesis of resolvins and protectins [13, 15]. In keeping with their broadened substrate scope the 12- and 15-lipoxygenases are known to be reactive towards intact phospholipids, and do not require their hydrolysis for peroxidation [17, 18]. …”
Section: Biological Synthesis Of Lipid Peroxidesmentioning
confidence: 99%
“…Generally, free polyunsaturated fatty acids are preferred as substrates for LOXs [1,[2][3][4]. Nonetheless, there have been reports [5][6][7][8][9][10][11][12][13][14] that certain plant LOXs can oxidize phospholipids [5][6][7] or triglycerides [8]. Additionally, mammalian LOXs such as reticulocyte LOX or leukocyte-type LOX (12-LOX) oxygenate complex substrates such as phospholipids or biomembranes [9][10][11][12][13][14].…”
Section: Introductionmentioning
confidence: 99%