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Arginine is the amino acid with the formula (H 2 N)(HN)CN(H)(CH 2) 3 CH(NH 2)CO 2 H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO 2 − ) and both the amino and guanidino groups are protonated, resulting in a cation.
Chemical formula: C 6 H 14 N 4 O 2 Molar mass: 174.2 g·mol −1 Systematic name: 2-amino-5-(diaminomethylidene amino)pentanoic acid Abbreviations: R, Arg Synonyms: 2-amino-5-guanidinopentanoic acid 2-amino-5-guanidinovaleric acid AIDS{-}121865 AIDS{-}159840 Argamine Arginin Argivene CHEBI:29016 CHEMBANK2983 Detoxargin Harg Levargin Minophagen ...
Functional groups found in histidine (left), lysine (middle) and arginine (right) There are three amino acids with side chains that are cations at neutral pH: arginine (Arg, R), lysine (Lys, K) and histidine (His, H). Arginine has a charged guanidino group and lysine a charged alkyl amino group, and are fully protonated at pH 7.
Lysine ball and stick model spinning. Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.Lysine contains an α-amino group (which is in the protonated −NH + 3 form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated −COO − form when the lysine is dissolved in water at physiological pH ...
The chemical conversion of arginine to citrulline, known as citrullination or deimination. Citrullination or deimination is the conversion of the amino acid arginine in a protein into the amino acid citrulline. Citrulline is not one of the 20 standard amino acids encoded by DNA in the genetic code.
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]
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]
Additionally, 2(S)-amino-6-boronohexonic acid (ABH) is an L-arginine analogue that also creates a tetrahedral intermediate similar to that formed in the catalysis of the natural substrate, and is a potent inhibitor of human arginase I. [7]
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