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1.11.1.12: phospholipid-hydroperoxide glutathione peroxidase

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

Word Map on EC 1.11.1.12

Reaction

2 glutathione +

a hydroperoxy-fatty-acyl-[lipid]
=
glutathione disulfide
+
a hydroxy-fatty-acyl-[lipid]
+
H2O

Synonyms

AC-PHGPx, Bi-PHGPx, class 4 GPx, CsGPx1, CsGPx2, CsGPx3, CsGPx4, DMPHGPx, glutathione peroxidase 4, glutathione peroxidase-4, glutathione-dependent phospholipid peroxidase, GPX, GPx-4, GPX3, GPx4, GPx41, GPx4A, GPx4B, GPXhs2, GPXle1, hydroperoxide glutathione peroxidase, Hyr1, Hyr1/YIR037W, McPHGPx, More, non-selenocysteine PHGPx, NPGPx, nPHGPx, OsPHGPx, peroxidation-inhibiting protein, peroxidation-inhibiting protein: peroxidase, glutathione (phospholipid hydroperoxide-reducing), PHGPX, phospholipid glutathione peroxidase, phospholipid hydroperoxidase, phospholipid hydroperoxide glutathione peroxidase, phospholipid hydroperoxide glutathione peroxidase A, phospholipid hydroperoxide glutathione peroxidase B, phospholipid hydroperoxide glutathione peroxidase-4, phospholipid-hydroperoxide glutathione peroxidase, selenium-dependent glutathione peroxidase type-4, seleno GPx, selenoperoxidase, selenoprotein P, sperm nucleus-specific glutathione peroxidase, TTHERM_00661720, type-4 glutathione peroxidase, VcPHGPx

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase

Crystallization

Crystallization on EC 1.11.1.12 - phospholipid-hydroperoxide glutathione peroxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of mutant C2S/C10S/C37S/C66S/C75S/C107S/C148S. The catalytic tetrad consists of residues Sec46, Gln81, Trp136, and Asn137
sparse matrix crystallization method, crystal structure of the catalytically active U46C mutant of human GPx4 to 1.55 A resolution
structure of recombinant protein, at 1.3 A resolution. Data indicate a monomeric protein, which contains the catalytic selenium at the redox level of the seleninic acid. The presumed catalytic triad consists of residues Sec(Cys)46, Gln81 and Trp136. The triad is localized at a flat impression of the protein surface
structure of the wild-type form of GPX4 at 1.0 A resolution and in complex with inhibitor 2-chloro-N-(3-chloro-4-methoxyphenyl)-N-[(1S)-2-(phenylethylethylamino)-2-oxo-1-(thiophen-2-yl)ethyl]acetamide. Active site residue is Sec46
crystal structure of the selenocysteine 46 to cysteine mutant, residues Met1 to Leu170, to 1.8 A resolution
the crystal structure is solved to a resolution of 2.0 A
-
the crystal structures of the Sec43Cys and Sec43Ser mutants are solved at resolutions of 1.0 A and 1.7 A, respectively
-