Selenocysteine
Chemical compound / From Wikipedia, the free encyclopedia
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Selenocysteine (symbol Sec or U,[4] in older publications also as Se-Cys)[5] 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.
Names | |
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IUPAC name
Selenocysteine | |
Systematic IUPAC name
3-Selanyl-L-alanine (semisystematic name)
2-Amino-3-selanylpropanoic acid (fully systematic name) | |
Other names
L-Selenocysteine; Selenium-cysteine | |
Identifiers | |
3D model (JSmol) |
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ChEBI | |
ChEMBL | |
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DrugBank |
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ECHA InfoCard | 100.236.386 |
KEGG |
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PubChem CID |
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UNII | |
CompTox Dashboard (EPA) |
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Properties | |
C3H7NO2Se | |
Molar mass | 168.065 g·mol−1 |
Properties | |
Acidity (pKa) | 5.24,[2] 5.43[3] |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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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.[6]
Selenocysteine was discovered in 1974[7] by biochemist Thressa Stadtman at the National Institutes of Health.[8]