Selenocysteine

Selenocysteine
Names
IUPAC name
Selenocysteine
Systematic IUPAC name
2-Amino-3-selanylpropanoic acid
Other names
L-Selenocysteine; Selenium-cysteine
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.236.386
KEGG
UNII
  • InChI=1S/C3H7NO2Se/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 Y
    Key: ZKZBPNGNEQAJSX-REOHCLBHSA-N Y
  • InChI=1/C3H7NO2Se/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
    Key: ZKZBPNGNEQAJSX-REOHCLBHBZ
  • O=C(O)[C@@H](N)C[SeH]
  • Zwitterion: O=C([O-])[C@@H]([NH3+])C[SeH]
Properties
C3H7NO2Se
Molar mass 168.065 g·mol−1
Properties
Acidity (pKa) 5.24, 5.43
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
N verify (what is YN ?)
Infobox references

Selenocysteine (symbol Sec or U, in older publications also as Se-Cys) is the 21st proteinogenic amino acid. Selenoproteins contain selenocysteine residues. Selenocysteine is an analogue of the more common cysteine with selenium in place of the sulfur.

Selenocysteine is present in several enzymes (for example glutathione peroxidases, tetraiodothyronine 5′ deiodinases, thioredoxin reductases, formate dehydrogenases, glycine reductases, selenophosphate synthetase 2, methionine-R-sulfoxide reductase B1 (SEPX1), and some hydrogenases). It occurs in all three domains of life, including important enzymes (listed above) present in humans.

Selenocysteine was discovered in 1974 by biochemist Thressa Stadtman at the National Institutes of Health.