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|Section2= |Section3= }} Selenocysteine (abbreviated as Sec or U, in older publications also as Se-Cys) is the 21st proteinogenic amino acid. Selenocysteine exists naturally in all kingdoms of life as a building block of selenoproteins. Selenocysteine is a cysteine analogue with a selenium-containing selenol group in place of the sulfur-containing thiol group. 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). Selenocysteine was discovered by biochemist Thressa Stadtman at the National Institutes of Health. ==Structure== Selenocysteine has a structure similar to that of cysteine, but with an atom of selenium taking the place of the usual sulfur, forming a selenol group which is deprotonated at physiological pH. Proteins that contain one or more selenocysteine residues are called selenoproteins and those with catalytic activities which depend on selenocysteine's biochemical activity are called selenoenzymes. The structurally characterized selenoenzymes have been found to employ catalytic triad structures that influence the nucleophilicity of the active site selenocysteine. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Selenocysteine」の詳細全文を読む スポンサード リンク
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