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- Name help_outline (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate Identifier CHEBI:57444 Charge -1 Formula C20H31O4 InChIKeyhelp_outline ZIOZYRSDNLNNNJ-LQWMCKPYSA-M SMILEShelp_outline CCCCC\C=C/C[C@H](OO)\C=C\C=C/C\C=C/CCCC([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 (8R)-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate Identifier CHEBI:75233 Charge -1 Formula C20H31O4 InChIKeyhelp_outline SGTUOBURCVMACZ-MEVKQHDMSA-M SMILEShelp_outline CCCCC\C=C/C[C@@H]1O[C@H]1\C=C\[C@H](O)C\C=C/CCCC([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:37955 | RHEA:37956 | RHEA:37957 | RHEA:37958 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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The lipoxygenase gene ALOXE3 implicated in skin differentiation encodes a hydroperoxide isomerase.
Yu Z., Schneider C., Boeglin W.E., Marnett L.J., Brash A.R.
Lipoxygenase (LOX) enzymes form fatty acid hydroperoxides used in membrane remodeling and cell signaling. Mammalian epidermal LOX type 3 (eLOX3) is distinctive in totally lacking this typical oxygenase activity. Surprisingly, genetic evidence has linked mutations in eLOX3 or a colocalizing enzyme, ... >> More
Lipoxygenase (LOX) enzymes form fatty acid hydroperoxides used in membrane remodeling and cell signaling. Mammalian epidermal LOX type 3 (eLOX3) is distinctive in totally lacking this typical oxygenase activity. Surprisingly, genetic evidence has linked mutations in eLOX3 or a colocalizing enzyme, 12R-LOX, to disruption of the normal permeability barrier of the skin [Jobard, F., Lefèvre, C., Karaduman, A., Blanchet-Bardon, C., Emre, S., Weissenbach, J., Ozgüc, M., Lathrop, M., Prud'homme, J. F. & Fischer, J. (2002) Hum. Mol. Genet. 11, 107-113]. Herein we identify a logical link of the biochemistry to the genetics. eLOX3 functions as a hydroperoxide isomerase (epoxyalcohol synthase) by using the product of 12R-LOX as the preferred substrate. 12R-Hydroperoxyeicosatetraenoic acid (12R-HPETE) is converted to 8R-hydroxy-11R,12R-epoxyeicosa-5Z,9E,14Z-trienoic acid, one of the isomers of hepoxilin A3, and to 12-ketoeicosatetraenoic acid in a 2:1 ratio. Other hydroperoxides, including 8R-HPETE, 12S-HPETE, and 15S-HPETE, as well as the 13S- and 13R-hydroperoxides of linoleic acid are converted less efficiently. Mass spectrometric analysis of the epoxyalcohol formed from [18O]15S-HPETE showed that both hydroperoxy oxygens are retained in the product. We propose that the ferrous form of eLOX3 initiates a redox cycle, unprecedented among LOX in being autocatalytic, in which the hydroperoxy substrate is isomerized to the epoxyalcohol or keto product. Our results provide strong biochemical evidence for a functional linkage of 12R-LOX and eLOX3 and clues into skin biochemistry and the etiology of ichthyosiform diseases in humans. << Less
Proc. Natl. Acad. Sci. U.S.A. 100:9162-9167(2003) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.