Enzymes
| UniProtKB help_outline | 3 proteins |
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- Name help_outline (13S)-hydroperoxy-(9Z,11E)-octadecadienoate Identifier CHEBI:57466 (Beilstein: 10594821) help_outline Charge -1 Formula C18H31O4 InChIKeyhelp_outline JDSRHVWSAMTSSN-IRQZEAMPSA-M SMILEShelp_outline CCCCC[C@H](OO)\C=C\C=C/CCCCCCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 11-hydroxy-(12S,13S)-epoxy-(9Z)-octadecenoate Identifier CHEBI:132064 Charge -1 Formula C18H31O4 InChIKeyhelp_outline UZCLYICSWADYGM-VHIAHCGJSA-M SMILEShelp_outline C(CCCCCCC/C=C\C([C@H]1[C@H](CCCCC)O1)O)(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:50212 | RHEA:50213 | RHEA:50214 | RHEA:50215 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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On the role of molecular oxygen in lipoxygenase activation: comparison and contrast of epidermal lipoxygenase-3 with soybean lipoxygenase-1.
Zheng Y., Brash A.R.
The oxygenation of polyunsaturated fatty acids by lipoxygenases (LOX) is associated with a lag phase during which the resting ferrous enzyme is converted to the active ferric form by reaction with fatty acid hydroperoxide. Epidermal lipoxygenase-3 (eLOX3) is atypical in displaying hydroperoxide is ... >> More
The oxygenation of polyunsaturated fatty acids by lipoxygenases (LOX) is associated with a lag phase during which the resting ferrous enzyme is converted to the active ferric form by reaction with fatty acid hydroperoxide. Epidermal lipoxygenase-3 (eLOX3) is atypical in displaying hydroperoxide isomerase activity with fatty acid hydroperoxides through cycling of the ferrous enzyme. Yet eLOX3 is capable of dioxygenase activity, albeit with a long lag phase and need for high concentrations of hydroperoxide activator. Here, we show that higher O(2) concentration shortens the lag phase in eLOX3, although it reduces the rate of hydroperoxide consumption, effects also associated with an A451G mutation known to affect the disposition of molecular oxygen in the LOX active site. These observations are consistent with a role of O(2) in interrupting hydroperoxide isomerase cycling. Activation of eLOX3, A451G eLOX3, and soybean LOX-1 with 13-hydroperoxy-linoleic acid forms oxygenated end products, which we identified as 9R- and 9S-hydroperoxy-12S,13S-trans-epoxyoctadec-10E-enoic acids. We deduce that activation partly depends on reaction of O(2) with the intermediate of hydroperoxide cleavage, the epoxyallylic radical, giving an epoxyallylic peroxyl radical that does not further react with Fe(III)-OH; instead, it dissociates and leaves the enzyme in the activated free ferric state. eLOX3 differs from soybean LOX-1 in more tightly binding the epoxyallylic radical and having limited access to O(2) within the active site, leading to a deficiency in activation and a dominant hydroperoxide isomerase activity. << Less
J. Biol. Chem. 285:39876-39887(2010) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.