Family

Glutathione peroxidase (IPR000889)

Short name: Glutathione_peroxidase

Family relationships

Description

Glutathione peroxidase (GSHPx) (EC:1.11.1.9) 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 Escherichia coli protein btuE, a periplasmic protein involved in vitamin B12 transport, is evolutionarily related to GSHPxs, although the significance of this relationship is unclear. The structure of bovine seleno-glutathione peroxidase has been determined [PMID: 6852035]. The protein belongs to the alpha-beta class, with a 3 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.
PANTHER
PRINTS
PROSITE profiles
PIRSF
Pfam