Glutathione peroxidase 3

Enzyme in humans From Wikipedia, the free encyclopedia

Glutathione peroxidase 3

Glutathione peroxidase 3 (GPx-3), also known as plasma glutathione peroxidase (GPx-P) or extracellular glutathione peroxidase is an enzyme that in humans is encoded by the GPX3 gene.[5][6][7]

Quick Facts GPX3, Available structures ...
GPX3
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Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGPX3, GPx-P, GSHPx-3, GSHPx-P, glutathione peroxidase 3
External IDsOMIM: 138321; MGI: 105102; HomoloGene: 20480; GeneCards: GPX3; OMA:GPX3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002084
NM_001329790

NM_001083929
NM_008161
NM_001329860

RefSeq (protein)

NP_001316719
NP_002075

NP_001316789
NP_032187

Location (UCSC)Chr 5: 151.02 – 151.03 MbChr 11: 54.79 – 54.8 Mb
PubMed search[3][4]
Wikidata
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GPx-3 belongs to the glutathione peroxidase family, which functions in the detoxification of hydrogen peroxide. It contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon, which normally signals translation termination. The 3' UTR of Sec-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal.[5]

Thiol specificity

GPx-3 has a wide thiol specificity. The sources of reducing power for GPx-3 in vitro include GSH, cysteine, mercaptoethanol, and dithiothreitol.[8] There is an evidence of effectiveness of homocysteine in reduction of GPx-3: GSH can be completely replaced by reduced homocysteine in vitro.[9][10]

Changes during ontogeny

In the rat blood plasma, the GPx-3 activity is low during the first two weeks after birth and rapidly increasing during transition from milk nutrition to solid food. Aging is accompanied by decrease in GPx-3 activity: in the blood plasma of rats it occurs around 23-26 months of age.[10]

References

Further reading

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