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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 ...
The enzyme threonine synthase (EC 4.2.3.1) catalyzes the chemical reaction O -phospho- L -homoserine + H 2 O ⇌ {\displaystyle \rightleftharpoons } L -threonine + phosphate This enzyme belongs to the family of lyases , specifically those carbon-oxygen lyases acting on phosphates.
The synthesis of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, is feed-back inhibited by lysine, isoleucine, and threonine, which prevents the synthesis of the amino acids derived from aspartate. So, in addition to inhibiting the first enzyme of the aspartate ...
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.
Serine and threonine have a short group ended with a hydroxyl group. Its hydrogen is easy to remove, so serine and threonine often act as hydrogen donors in enzymes. Both are very hydrophilic, so the outer regions of soluble proteins tend to be rich with them. Threonine: T Thr Essential for humans, Thr behaves similarly to serine ...
Sites that often undergo post-translational modification are those that have a functional group that can serve as a nucleophile in the reaction: the hydroxyl groups of serine, threonine, and tyrosine; the amine forms of lysine, arginine, and histidine; the thiolate anion of cysteine; the carboxylates of aspartate and glutamate; and the N- and C ...
Pseudoproline dipeptides have proven particularly effective in the synthesis of intractable peptides, long peptides/small proteins, and cyclic peptides, enabling in many cases the production of peptides that otherwise could not be made. These dipeptides are extremely easy to use: simply substitute a serine or threonine residue together with the ...
Cyanosulfidic prebiotic synthesis is a proposed mechanism for the origin of the key chemical building blocks of life. [1] It involves a systems chemistry approach to synthesize the precursors of amino acids , ribonucleotides , and lipids using the same starting reagents and largely the same plausible early Earth conditions. [ 2 ]