Glutathione peroxidase active site
IPR029759
Definition
The catalytic site of glutathione peroxidases contains a conserved residue which is either a cysteine or, in many eukaryotic glutathione peroxidase, a selenocysteine PMID:2142875. This entry represents the region around this active site residue. 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. 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.
7 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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