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Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation from RNA. 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 ...
The 21 proteinogenic α-amino acids found in eukaryotes, grouped according to their side chains' pK a values and charges carried at physiological pH (7.4) 2-, alpha-, or α-amino acids [21] have the generic formula H 2 NCHRCOOH in most cases, [b] where R is an organic substituent known as a "side chain". [22]
Pages in category "Proteinogenic amino acids" The following 24 pages are in this category, out of 24 total. This list may not reflect recent changes. ...
Cysteine (/ ˈ s ɪ s t ɪ iː n /; [5] symbol Cys or C [6]) is a semiessential [7] proteinogenic amino acid with the formula HOOC−CH(−NH 2)−CH 2 −SH. The thiol side chain in cysteine enables the formation of disulfide bonds , and often participates in enzymatic reactions as a nucleophile .
Threonine was the last of the 20 common proteinogenic amino acids to be discovered. It was discovered in 1935 by William Cumming Rose, [7] collaborating with Curtis Meyer. The amino acid was named threonine because it was similar in structure to threonic acid, a four-carbon monosaccharide with molecular formula C 4 H 8 O 5 [8]
Proline (symbol Pro or P) [4] is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group-NH 2 but is rather a secondary amine.
Glycine (symbol Gly or G; [6] / ˈ ɡ l aɪ s iː n / ⓘ) [7] is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). [8]
Aside from being a proteinogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. Its hydroxy group is able to form the ester linkage, with phosphate in particular. Phosphate groups are transferred to tyrosine residues by way of protein kinases. This is one of the post-translational modifications.