The Description of Threonine
The Description of Threonine
Threonine (abbreviated as Thr or T) is an α-amino acid with the chemical formula HO2CCH(NH2)CH(OH)CH3. Its codons are ACU, ACA, ACC, and ACG. This essential amino acid is classified as polar. 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.
The threonineresidue is susceptible to numerous posttranslational modifications. The hydroxy 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.
Threonine was discovered as the last of the 20 common proteinogenic amino acids in the 1930s by William Cumming Rose.
The threonineresidue is susceptible to numerous posttranslational modifications. The hydroxy 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.
Threonine was discovered as the last of the 20 common proteinogenic amino acids in the 1930s by William Cumming Rose.