Biology:GPX3

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Short description: Enzyme in humans


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

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.[1][2][3]

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.[1]

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.[4] There is an evidence of effectiveness of homocysteine in reduction of GPx-3: GSH can be completely replaced by reduced homocysteine in vitro.[5][6]

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.[6]

References

  1. 1.0 1.1 "Entrez Gene: glutathione peroxidase 3 (plasma)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2878. 
  2. "Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme". Archives of Biochemistry and Biophysics 256 (2): 677–86. August 1987. doi:10.1016/0003-9861(87)90624-2. PMID 3619451. 
  3. "The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to chromosomes 14, 5, and 19, respectively". Cytogenetics and Cell Genetics 66 (2): 96–8. 1994. doi:10.1159/000133675. PMID 8287691. 
  4. "A comparative study on the hydroperoxide and thiol specificity of the glutathione peroxidase family and selenoprotein P". The Journal of Biological Chemistry 277 (43): 41254–8. October 2002. doi:10.1074/jbc.M202773200. PMID 12185074. 
  5. "[Thiol peroxidase activities in rat blood plasma determined with hydrogen peroxide and 5,5'-dithio-bis(2-nitrobenzoic acid)]". Biomeditsinskaia Khimiia 62 (4): 431–8. May 2016. doi:10.18097/PBMC20166204431. PMID 27562997. 
  6. 6.0 6.1 "Changes in the Activity of Glutathione Peroxidase in the Blood Plasma and Serum of Rats during Postnatal Development and Aging". Advances in Gerontology 9 (3): 283–288. 2019. doi:10.1134/s2079057019030147. 

Further reading

External links

  • Overview of all the structural information available in the PDB for UniProt: P22352 (Glutathione peroxidase 3) at the PDBe-KB.