Glutathione peroxidase (IPR000889)

Short name: Glutathione_peroxidase

Overlapping homologous superfamilies

Family relationships


Glutathione peroxidase (GSHPx) (EC: is an enzyme that catalyses the reduction of hydroxyperoxides by glutathione [PMID: 7565867]. Its main function is to protect against the damaging effect of endogenously formed hydroxyperoxides. In higher vertebrates, several forms of GSHPx are known, including a ubiquitous cytosolic form (GSHPx-1), a gastrointestinal cytosolic form (GSHPx-GI), a plasma secreted form (GSHPx-P), and an epididymal secretory form (GSHPx-EP). In addition to these characterised forms, the sequence of a protein of unknown function [PMID: 2771650] has been shown to be evolutionary related to those of GSHPx's.

In filarial nematode parasites, the major soluble cuticular protein (gp29) is a secreted GSHPx, which may provide a mechanism of resistance to the immune reaction of the mammalian host by neutralising the products of the oxidative burst of leukocytes [PMID: 1631065]. The structure of bovine seleno-glutathione peroxidase has been determined [PMID: 6852035]. The protein belongs to the alpha-beta class, with a three layer(aba) sandwich architecture. The catalyic site of GSHPx contains a conserved residue which is either a cysteine or, in many eukaryotic GSHPx, a selenocysteine [PMID: 2142875].

GO terms

Biological Process

GO:0055114 oxidation-reduction process
GO:0006979 response to oxidative stress

Molecular Function

GO:0004602 glutathione peroxidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles