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  2. Threonine - Wikipedia

    en.wikipedia.org/wiki/Threonine

    Threonine (symbol Thr or T) [2] is an amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated −NH + 3 form when dissolved in water), a carboxyl group (which is in the deprotonated −COO − form when dissolved in water), and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid.

  3. Allothreonine - Wikipedia

    en.wikipedia.org/wiki/Allothreonine

    Allothreonine. Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Allothreonine is an amino acid with the formula CH3CH (OH)CH (NH2)CO2H. It is the diastereomer of the amino acid threonine. Like most other amino acids, allothreonine is a water-soluble colorless solid.

  4. Diastereomer - Wikipedia

    en.wikipedia.org/wiki/Diastereomer

    There are many more pairs of diastereomers, because each of these configurations is a diastereomer with respect to every other configuration excluding its own enantiomer (for example, R,R,R is a diastereomer of R,R,S; R,S,R; and R,S,S). For n = 4, there are sixteen stereoisomers, or eight pairs of enantiomers.

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    This is an example of severe perturbation, and is not characteristic of serine residues in general. Threonine has two chiral centers, not only the L (2S) chiral center at the α-carbon shared by all amino acids apart from achiral glycine, but also (3R) at the β-carbon. The full stereochemical specification is (2S,3R)-L-threonine.

  6. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation. The word "proteinogenic" means "protein creating". Throughout known life, there are 22 genetically encoded (proteinogenic) amino acids, 20 in the standard genetic code and an additional 2 (selenocysteine and pyrrolysine) that can ...

  7. O-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/O-linked_glycosylation

    O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational modification that occurs after the protein has been synthesised. In eukaryotes, it occurs in the endoplasmic reticulum, Golgi apparatus and occasionally in the ...

  8. TGF beta receptor - Wikipedia

    en.wikipedia.org/wiki/TGF_beta_receptor

    Domains. InterPro. Transforming growth factor beta (TGFβ) receptors are single pass serine/threonine kinase receptors that belong to TGFβ receptor family. They exist in several different isoforms that can be homo - or heterodimeric. [1] The number of characterized ligands in the TGFβ superfamily far exceeds the number of known receptors ...

  9. Serine/threonine-specific protein kinase - Wikipedia

    en.wikipedia.org/wiki/Serine/threonine-specific...

    Many serine/threonine protein kinases do not have their own individual EC numbers and use 2.7.11.1, "non-specific serine/threonine protein kinase". This entry is for any enzyme that phosphorylates proteins while converting ATP to ADP (i.e., ATP:protein phosphotransferases.) [10] 2.7.11.37 "protein kinase" was the former generic placeholder and was split into several entries (including 2.7.11.1 ...