RHEA:37948
| Reaction with net flow from left to right. help_outline | |
| Enzymes help_outline | 427 proteins (UniProtKB) |
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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 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate Identifier CHEBI:75231 Charge -1 Formula C20H29O3 InChIKeyhelp_outline GURBRQGDZZKITB-VXBMJZGYSA-M SMILEShelp_outline CCCCC\C=C/CC(=O)\C=C\C=C/C\C=C/CCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 5,139 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Links to other resources
| RHEA:37947 | RHEA:37948 | RHEA:37949 | RHEA:37950 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Citations
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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.