Active Site

Glutathione peroxidase active site (IPR029759)

Short name: GPX_AS


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.

Escherichia coli protein btuE, a periplasmic protein involved in the transport of vitamin B12, is also evolutionary related to GSHPx's; the significance of this relationship is not yet clear.

The catalyic site of GSHPx contains a conserved residue which is either a cysteine or, in many eukaryotic GSHPx, a selenocysteine [PMID: 2142875]. This entry represents the region around this active site residue.

Contributing signatures

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