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- Name help_outline (11S)-hydroperoxy-(9Z,12Z)-octadecadienoate Identifier CHEBI:57467 Charge -1 Formula C18H31O4 InChIKeyhelp_outline PLWDMWAXENHPLY-PDBSFCERSA-M SMILEShelp_outline CCCCC\C=C/[C@H](OO)\C=C/CCCCCCCC([O-])=O 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 (13R)-hydroperoxy-(9Z,11E)-octadecadienoate Identifier CHEBI:133985 Charge -1 Formula C18H31O4 InChIKeyhelp_outline JDSRHVWSAMTSSN-PIHGWCCBSA-M SMILEShelp_outline C(CCCCCCC\C=C/C=C/[C@@H](CCCCC)OO)(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:51304 | RHEA:51305 | RHEA:51306 | RHEA:51307 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Expression and characterization of manganese lipoxygenase of the rice blast fungus reveals prominent sequential lipoxygenation of alpha-linolenic acid.
Wennman A., Jerneren F., Magnuson A., Oliw E.H.
Magnaporthe oryzae causes rice blast disease and has become a model organism of fungal infections. M. oryzae can oxygenate fatty acids by 7,8-linoleate diol synthase, 10R-dioxygenase-epoxy alcohol synthase, and by a putative manganese lipoxygenase (Mo-MnLOX). The latter two are transcribed during ... >> More
Magnaporthe oryzae causes rice blast disease and has become a model organism of fungal infections. M. oryzae can oxygenate fatty acids by 7,8-linoleate diol synthase, 10R-dioxygenase-epoxy alcohol synthase, and by a putative manganese lipoxygenase (Mo-MnLOX). The latter two are transcribed during infection. The open reading frame of Mo-MnLOX was deduced from genome and cDNA analysis. Recombinant Mo-MnLOX was expressed in Pichia pastoris and purified to homogeneity. The enzyme contained protein-bound Mn and oxidized 18:2n-6 and 18:3n-3 to 9S-, 11-, and 13R-hydroperoxy metabolites by suprafacial hydrogen abstraction and oxygenation. The 11-hydroperoxides were subject to β-fragmentation with formation of 9S- and 13R-hydroperoxy fatty acids. Oxygen consumption indicated apparent kcat values of 2.8 s(-1) (18:2n-6) and 3.9 s(-1) (18:3n-3), and UV analysis yielded apparent Km values of 8 and 12 μM, respectively, for biosynthesis of cis-trans conjugated metabolites. 9S-Hydroperoxy-10E,12Z,15Z-octadecatrienoic acid was rapidly further oxidized to a triene, 9S,16S-dihydroperoxy-10E,12Z,14E-octadecatrienoic acid. In conclusion, we have expressed, purified and characterized a new MnLOX from M. oryzae. The pathogen likely secretes Mo-MnLOX and phospholipases to generate oxylipins and to oxidize lipid membranes of rice cells and the cuticle. << Less
Arch. Biochem. Biophys. 583:87-95(2015) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.
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Manganese lipoxygenase. Discovery of a bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction.
Hamberg M., Su C., Oliw E.
Linoleic acid was incubated with manganese lipoxygenase (Mn-LO) from the fungus Gäumannomyces graminis. The product consisted of (13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid ((13R)-HPOD) and a new hydroperoxide, (11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid ((11S)-HPOD). Incubation of (11R)-[ ... >> More
Linoleic acid was incubated with manganese lipoxygenase (Mn-LO) from the fungus Gäumannomyces graminis. The product consisted of (13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid ((13R)-HPOD) and a new hydroperoxide, (11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid ((11S)-HPOD). Incubation of (11R)-[2H]- and (11S)-[2H]linoleic acids with Mn-LO led to the formation of hydroperoxides that largely retained and lost, respectively, the deuterium label. Conversion of the (11S)-deuteriolinoleic acid was accompanied by a primary isotope effect, which manifested itself in a strongly reduced rate of formation of hydroperoxides and in a time-dependent accumulation of deuterium in the unconverted substrate. These experiments indicated that the initial step catalyzed by Mn-LO consisted of abstraction of the pro-S hydrogen of linoleic acid to produce a linoleoyl radical. (11S)-HPOD was converted into (13R)-HPOD upon incubation with Mn-LO. The mechanism of this enzyme-catalyzed hydroperoxide rearrangement was studied in experiments carried out with 18O2 gas or 18O2-labeled hydroperoxides. Incubation of [11-18O2](11S)-HPOD with Mn-LO led to the formation of (13R)-HPOD, which retained 39-44% of the 18O label, whereas (11S)-HPOD incubated with Mn-LO under 18O2 produced (13R)-HPOD, which had incorporated 57% of 18O. Furthermore, analysis of the isotope content of (11S)-HPOD remaining unconverted in such incubations demonstrated that [11-18O2](11S)-HPOD suffered a time-dependent loss of 18O when exposed to Mn-LO, whereas (11S)-HPOD incorporated 18O when incubated with Mn-LO under 18O2. On the basis of these experiments, it was proposed that the conversion of (11S)-HPOD into (13R)-HPOD occurred in a non-concerted way by deoxygenation into a linoleoyl radical. Subsequent reoxygenation of this intermediate by dioxygen attack at C-13 produced (13R)-HPOD, whereas attack at C-11 regenerated (11S)-HPOD. The hydroperoxide rearrangement occurred by oxygen rebound, although, as demonstrated by the 18O experiments, the oxygen molecule released from (11S)-HPOD exchanged with surrounding molecular oxygen prior to its reincorporation. << Less
J Biol Chem 273:13080-13088(1998) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.