Selenoprotein

In molecular biology a selenoprotein is any protein that includes a selenocysteine (Sec, U, Se-Cys) amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec.[1] Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Sec residues, which are split into two domains, a longer N-terminal domain that contains 1 Sec, and a shorter C-terminal domain that contains 9 Sec. The longer N-terminal domain is likely an enzymatic domain, and the shorter C-terminal domain is likely a means of safely transporting the very reactive selenium atom throughout the body.[2][3]

  1. ^ Hatfield DL; Gladyshev VN (June 2002). "How selenium has altered our understanding of the genetic code". Mol. Cell. Biol. 22 (11): 3565–76. doi:10.1128/MCB.22.11.3565-3576.2002. PMC 133838. PMID 11997494.
  2. ^ Burk RF; Hill KE (2005). "Selenoprotein P: an extracellular protein with unique physical characteristics and a role in selenium homeostasis". Annu Rev Nutr. 25: 215–235. doi:10.1146/annurev.nutr.24.012003.132120. PMID 16011466.
  3. ^ Burk RF; Hill KE (2009). "Selenoprotein P-expression, functions, and roles in mammals". Biochim Biophys Acta. 1790 (11): 1441–1447. doi:10.1016/j.bbagen.2009.03.026. PMC 2763998. PMID 19345254.