1.11.1.27: glutathione-dependent peroxiredoxin
This is an abbreviated version!
For detailed information about glutathione-dependent peroxiredoxin, go to the full flat file.
Word Map on EC 1.11.1.27
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1.11.1.27
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peroxiredoxins
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plasmodium
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falciparum
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malaria
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prxvi
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intraerythrocytic
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medicine
- 1.11.1.27
- peroxiredoxins
- plasmodium
- falciparum
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malaria
- prxvi
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intraerythrocytic
- medicine
Reaction
Synonyms
1-Cys peroxiredoxin, 1-Cys Prdx, 1-Cys Prx, 1-CysPrx, 2-Cys peroxiredoxin, 2-Cys peroxiredoxin TPx-1, EC 1.11.1.15, glutathione peroxidase, GPX, HI0572, peroxiredoxin 6, peroxiredoxin II, peroxiredoxin VI, Pf1-Cys-Prx, PGdx, Prdx6, Prx1, Prx3, Prx6, TPx-1
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 1.11.1.27 - glutathione-dependent peroxiredoxin
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hyperoxidation
hyperoxidation of peroxiredoxin 6 induces alteration from dimeric to oligomeric state
phosphoprotein
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MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6
phosphoprotein
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MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6
phosphoprotein
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MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6
phosphoprotein
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MAP kinase mediated phosphorylation of Prdx6 at residue T177, results in increased phospholipase A2 activity, but phosphorylation has no effect on the peroxidase activity of Prdx6