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1.11.1.9: glutathione peroxidase

This is an abbreviated version!
For detailed information about glutathione peroxidase, go to the full flat file.

Word Map on EC 1.11.1.9

Reaction

2 glutathione +

H2O2
=
glutathione disulfide
+ 2 H2O

Synonyms

2-SeCD, 3,3'-telluro-bis(proapne-3,1-diyl)adamantane carboxylate, 6P229, ADA-Te-OH, ARMEP24, AtGPX1, ATGPX3, c-GPx4, Cellular glutathione peroxidase, cgd3_460, cGPx, Cuticular glycoprotein GP29, DI29, ebselen, EGLP, Epididymis-specific glutathione peroxidase-like protein, Extracellular glutathione peroxidase, G-6137, Gastrointestinal glutathione peroxidase, glutathione peroxidase 1, glutathione peroxidase 2, glutathione peroxidase 3, glutathione peroxidase 4, glutathione peroxidase Gpx2, glutathione peroxidase Gpx3, glutathione peroxidase-1, glutathione peroxidase-2, glutathione peroxidase-3, glutathione peroxidase-4, glutathione-dependent peroxidase I, glutathione:hydrogen-peroxide oxidoreductase, GP30, GPRP, GPX, Gpx-1, GPx-2, GPx-3, GPx-4, GPx-5, GPx-6, GPx-7, GPx-8, GPX1, Gpx2, GPX3, GPx4, GPX5, GSH peroxidase, GSH-Px, GSHPx, GSHPx-GI, intracellular GpX, m-GPx4, Major androgen-regulated protein, Major surface antigen GP29, n-GPx4, Nt-SubC08, Odorant-metabolizing protein RY2D1, Os02g0664000, OsGPX5, peroxidase, glutathione, PGdx, pGPx, PHGPX, phospholipid glutathione peroxidase, phospholipid hydroperoxide glutathione peroxidase, phospholipid hydroperoxide glutathione peroxidase, nuclear form, phospholipid hydroperoxide Gpx, plasma glutathione peroxidase, prion protein Ure2, reduced glutathione peroxidase, Salt-associated protein, Se-GPx, Se-hGSTZ1-1, Se-scFv-B3, secreted GpX, SeGPx, selenium containing glutathione transferase zeta1-1, selenium-dependent glutathione peroxidase, selenium-glutathione peroxidase, seleno-dependent glutathione peroxidase 1, selenosubtilisin, snGPx, TcGPXI, TTHERM_00046090, TTHERM_00046110, TTHERM_01099010, Ure2

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.9 glutathione peroxidase

Crystallization

Crystallization on EC 1.11.1.9 - glutathione peroxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure
-
molecular modeling of mutant with all Cys residues changed to Ser
molecular modeling of the structure of seleno-hGPx2
hanging-drop vapour-diffusion method, 2.6 A resolution. The crystals are triclinic and belong to space group P1, with unit-cell parameters a = 38.187, b = 43.372, c = 56.870 A, alpha = 71.405, beta = 73.376, gamma = 89.633
-
sitting drop vapor diffusion method, using 0.2 M LiSO4,0.2 M sodium acetate, 24% (w/v) PEG 8000, pH 4.5 for mutant enzyme U43C and 0.2 M NaH2PO4, 0.1 M MES, 32% (w/v) PEG-MME 5000, pH 6.0 for mutant enzyme U43S
computational kinetic modeling of selenol zwitterion anion as a glutathione peroxidase nanomimic. In the first step of the reaction, seleninic acid is produced through deprotonating of the selenol zwitterion anion in the presence of the hydrogen peroxide. Seleninic acid reacts with a thiol to form selenylsulfide in the second step. In the last step, selenylsulfide is reduced by the second thiol and regenerates selenolate anion through disulfide formation. The energy barrier of this reaction is 11.7 kcal per mol
-
molecular docking study of interactions between 15 selenenylsulfide compounds that mimic glutathione peroxidase and the active site of glutathione reductase by molecular docking. The reduction of selenenylsulfide by glutathione reductase is important in GPx-like activity determination of GPx mimics
-