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- Name help_outline (15S)-hydroperoxy-(11Z,13E)-eicosadienoate Identifier CHEBI:144832 Charge -1 Formula C20H35O4 InChIKeyhelp_outline KEXNVBSLXJLOPR-XMSPSUPSSA-M SMILEShelp_outline C(C/C=C\C=C\[C@H](CCCCC)OO)CCCCCCCC(=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 glutathione Identifier CHEBI:57925 Charge -1 Formula C10H16N3O6S InChIKeyhelp_outline RWSXRVCMGQZWBV-WDSKDSINSA-M SMILEShelp_outline [NH3+][C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)[O-])C(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 104 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (15S)-hydroxy-(11Z,13E)-eicosadienoate Identifier CHEBI:195402 Charge -1 Formula C20H35O3 InChIKeyhelp_outline ZTRWPEHMGCHTIT-XMSPSUPSSA-M SMILEShelp_outline C(C/C=C\C=C\[C@H](CCCCC)O)CCCCCCCC(=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 glutathione disulfide Identifier CHEBI:58297 Charge -2 Formula C20H30N6O12S2 InChIKeyhelp_outline YPZRWBKMTBYPTK-BJDJZHNGSA-L SMILEShelp_outline [NH3+][C@@H](CCC(=O)N[C@@H](CSSC[C@H](NC(=O)CC[C@H]([NH3+])C([O-])=O)C(=O)NCC([O-])=O)C(=O)NCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 37 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 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:76711 | RHEA:76712 | RHEA:76713 | RHEA:76714 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Side-by-side comparison of recombinant human glutathione peroxidases identifies overlapping substrate specificities for soluble hydroperoxides.
Schwarz M., Loeser A., Cheng Q., Wichmann-Costaganna M., Schaedel P., Werz O., Arner E.S., Kipp A.P.
Five out of eight human glutathione peroxidases (GPXs) are selenoproteins, representing proteins that contain selenium as part of the amino acid selenocysteine. The GPXs are important for reducing hydroperoxides in a glutathione-consuming manner and thus regulate cellular redox homeostasis. GPX1, ... >> More
Five out of eight human glutathione peroxidases (GPXs) are selenoproteins, representing proteins that contain selenium as part of the amino acid selenocysteine. The GPXs are important for reducing hydroperoxides in a glutathione-consuming manner and thus regulate cellular redox homeostasis. GPX1, GPX2, and GPX4 represent the three main cytosolic GPXs, but they differ in their expression patterns with GPX1 and GPX4 being expressed ubiquitously, whereas GPX2 is mainly expressed in epithelial cells. GPX1 and GPX2 have been described to reduce soluble hydroperoxides, while GPX4 reduces complex lipid hydroperoxides, thus protecting cells from lipid peroxidation and ferroptosis. But most of these data are derived from cells that are devoid of one of the isoforms and thus, compensation or other cellular effects might affect the conclusions. So far, the use of isolated recombinant human selenoprotein glutathione peroxidases in pure enzyme assays has not been employed to study their substrate specificities side by side. Using recombinant GPX1, GPX2, and GPX4 produced in E. coli we here assessed their GPX activities by a NADPH-consuming glutathione reductase-coupled assay with 17 different peroxides (all at 50 μM) as substrates. GPX4 was clearly the only isoform able to reduce phosphatidylcholine hydroperoxide. In contrast, small soluble hydroperoxides such as H<sub>2</sub>O<sub>2</sub>, cumene hydroperoxide, and tert-butyl hydroperoxide were reduced by all three isoforms, but with approximately 10-fold higher efficiency for GPX1 in comparison to GPX2 and GPX4. Also, several fatty acid-derived hydroperoxides were reduced by all three isoforms and again GPX1 had the highest activity. Interestingly, the stereoisomerism of the fatty acid-derived hydroperoxides clearly affected the activity of the GPX enzymes. Overall, distinct substrate specificity is obvious for GPX4, but not so when comparing GPX1 and GPX2. Clearly GPX1 was the most potent isoform of the three GPXs in terms of turnover in reduction of soluble and fatty-acid derived hydroperoxides. << Less
Redox Biol. 59:102593-102593(2023) [PubMed] [EuropePMC]
This publication is cited by 14 other entries.