Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline (8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate Identifier CHEBI:57447 Charge -1 Formula C20H31O4 InChIKeyhelp_outline QQUFCXFFOZDXLA-GTYUHVKWSA-M SMILEShelp_outline CCCCC\C=C/C\C=C/C=C/[C@@H](C\C=C/CCCC([O-])=O)OO 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 8,9-epoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate Identifier CHEBI:134054 Charge -1 Formula C20H29O3 InChIKeyhelp_outline PVKOQJATMIOZNV-DXJGWMFSSA-M SMILEShelp_outline C(CCC/C=C\C[C@@H]1/C(/O1)=C/C=C\C/C=C\CCCCC)(=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
- Name help_outline H2O Identifier CHEBI:15377 (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 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:51344 | RHEA:51345 | RHEA:51346 | RHEA:51347 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Identification of a naturally occurring peroxidase-lipoxygenase fusion protein.
Koljak R., Boutaud O., Shieh B.-H., Samel N., Brash A.R.
A distant relative of catalase that is specialized for metabolism of a fatty acid hydroperoxide was identified. This heme peroxidase occurs in coral as part of a fusion protein, the other component of which is a lipoxygenase that forms the hydroperoxide substrate. The end product is an unstable ep ... >> More
A distant relative of catalase that is specialized for metabolism of a fatty acid hydroperoxide was identified. This heme peroxidase occurs in coral as part of a fusion protein, the other component of which is a lipoxygenase that forms the hydroperoxide substrate. The end product is an unstable epoxide (an allene oxide) that is a potential precursor of prostaglandin-like molecules. These results extend the known chemistry of catalase-like proteins and reveal a distinct type of enzymatic construct involved in the metabolism of polyunsaturated fatty acids. << Less
Science 277:1994-1996(1997) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide.
Oldham M.L., Brash A.R., Newcomer M.E.
8R-Lipoxygenase and allene oxide synthase (AOS) are parts of a naturally occurring fusion protein from the coral Plexaura homomalla. AOS catalyses the production of an unstable epoxide (an allene oxide) from the fatty acid hydroperoxide generated by the lipoxygenase activity. Here, we report the s ... >> More
8R-Lipoxygenase and allene oxide synthase (AOS) are parts of a naturally occurring fusion protein from the coral Plexaura homomalla. AOS catalyses the production of an unstable epoxide (an allene oxide) from the fatty acid hydroperoxide generated by the lipoxygenase activity. Here, we report the structure of the AOS domain and its striking structural homology to catalase. Whereas nominal sequence identity between the enzymes had been previously described, the extent of structural homology observed was not anticipated, given that this enzyme activity had been exclusively associated with the P450 superfamily, and conservation of a catalase fold without catalase activity is unprecedented. Whereas the heme environment is largely conserved, the AOS heme is planar and the distal histidine is flanked by two hydrogen-bonding residues. These critical differences likely facilitate the switch from a catalatic activity to that of a fatty acid hydroperoxidase. << Less
Proc. Natl. Acad. Sci. U.S.A. 102:297-302(2005) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.