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|Section2= |Section3= }} Threonine (abbreviated as Thr or T) is an essential, polar α-amino acid, with the formula HO2CCH(NH2)CH(OH)CH3. Together with serine, threonine is one of two proteinogenic amino acids bearing an alcohol group (tyrosine is not an alcohol but a phenol, since its hydroxyl group is bonded directly to an aromatic ring, giving it different acid/base and oxidative properties). It is also one of two common amino acids that bear a chiral side chain, along with isoleucine. Its codons are ACU, ACA, ACC, and ACG. The threonine residue is susceptible to numerous posttranslational modifications. The hydroxyl side-chain can undergo ''O''-linked glycosylation. In addition, threonine residues undergo phosphorylation through the action of a threonine kinase. In its phosphorylated form, it can be referred to as phosphothreonine. It is a precursor of glycine, and can be used as a prodrug to reliably elevate brain glycine levels. ==History== Threonine was discovered as the last of the 20 common proteinogenic amino acids in the 1930s by William Cumming Rose. 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「Threonine」の詳細全文を読む スポンサード リンク
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