GPX5: Human glutathione peroxidase 5
PDB Code: 2I3Y
Glutathione peroxidase 5 (GPX5) belongs to the glutathione peroxidase family, members of which are involved in scavenging and inactivating hydrogen and lipid peroxides to water or lipid hydroxyls in a glutathione-dependent reductive reaction. The GPX family therefore constitutes an important mechanism in the protection against oxidative stress. At this point, seven members of the GPX family were identified in humans with distinct catalytic properties and tissue-specific expression profiles.
The hallmark of the active site in GPX enzymes is the presence of a catalytically competent selenocysteine residue, rendering it highly active towards peroxides. GPX5 differs from most other members of the GPX family by the replacement of the selenocysteine residue by cysteine, and possibly as a result of this substitution GPX5 has lower peroxidase activity.
GPX5 is specifically expressed and secreted in the male reproductive tract. It is postulated that G PX5, which is bound to the acrosome of sperm, may act to protect sperm cells from a premature acrosome reaction in the epididymis and thus protect against peroxidative damage.
Differential splicing of exon 3 of the human GPX5 gene, which is located on chromosome 6p22.1, leads to two variant forms, one of which is lacking the active site residues. The majority of transcripts found in human reproductive tissue appears to have this deletion of exon 3.

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