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 hydroperoxide glutathione peroxidase, phospholipid hydroperoxide glutathione peroxidase A, phospholipid hydroperoxide glutathione peroxidase B, phospholipid hydroperoxide glutathione peroxidase-4, phospholipid-hydroperoxide glutathione peroxidase, phospholipid-hydroperoxide glutathione peroxidases, selenium-dependent glutathione peroxidase type-4, seleno GPx, selenoperoxidase, selenoprotein P, sperm nucleus-specific glutathione peroxidase, 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
-
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
-