In enzymology, a phospholipid-hydroperoxide glutathione peroxidase (EC 1.11.1.12) is an enzyme that catalyzes the chemical reaction
phospholipid-hydroperoxide glutathione peroxidase | |||||||||
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Identifiers | |||||||||
EC no. | 1.11.1.12 | ||||||||
CAS no. | 97089-70-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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- 2 glutathione + a lipid hydroperoxide glutathione disulfide + lipid + 2 H2O
Thus, the two substrates of this enzyme are glutathione and lipid hydroperoxide, whereas its 3 products are glutathione disulfide, lipid, and H2O.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is glutathione:lipid-hydroperoxide oxidoreductase. Other names in common use include peroxidation-inhibiting protein, PHGPX, peroxidation-inhibiting protein: peroxidase, glutathione, (phospholipid hydroperoxide-reducing), phospholipid hydroperoxide glutathione peroxidase, hydroperoxide glutathione peroxidase, or glutathione peroxidase 4 (GPX4). This enzyme participates in glutathione metabolism.
Structural studies
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2GS3 and 2OBI.
References
edit- Ursini F, Maiorino M, Gregolin C (1985). "The selenoenzyme phospholipid hydroperoxide glutathione peroxidase". Biochim. Biophys. Acta. 839 (1): 62–70. doi:10.1016/0304-4165(85)90182-5. PMID 3978121.