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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.
Cyclin-dependent kinases (CDKs) are a predominant group of serine/threonine protein kinases involved in the regulation of the cell cycle and its progression, ensuring the integrity and functionality of cellular machinery. These regulatory enzymes play a crucial role in the regulation of eukaryotic cell cycle and transcription, as well as DNA ...
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 (2 S ,3 R )- L - threonine .
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 ...
Propionyl-CoA is a coenzyme A derivative of propionic acid.It is composed of a 24 total carbon chain (without the coenzyme, it is a 3 carbon structure) and its production and metabolic fate depend on which organism it is present in. [1] Several different pathways can lead to its production, such as through the catabolism of specific amino acids or the oxidation of odd-chain fatty acids. [2]
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.
Checkpoint kinase 1, commonly referred to as Chk1, is a serine/threonine-specific protein kinase that, in humans, is encoded by the CHEK1 gene. [5][6] Chk1 coordinates the DNA damage response (DDR) and cell cycle checkpoint response. [7] Activation of Chk1 results in the initiation of cell cycle checkpoints, cell cycle arrest, DNA repair and ...
Serine and threonine phosphates are stable under physiological conditions, so a phosphatase enzyme has to remove the phosphate to reverse the regulation signal. Ser/Thr-specific protein phosphatases are regulated partly by their location within the cell and by specific inhibitor proteins.