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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 (carbamic acid is unstable). Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). [8]
It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865 by Emil Cramer. [5] Its name is derived from the Latin for silk, sericum. Serine's structure was established in 1902. [6] [7]
It is an amino acid derivative, naturally produced in the human body from the amino acids glycine and arginine, with an additional requirement for S-adenosyl methionine (a derivative of methionine) to catalyze the transformation of guanidinoacetate to creatine.
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Alanine is the simplest α-amino acid after glycine. The methyl side-chain of alanine is non-reactive and is therefore hardly ever directly involved in protein function. [12] Alanine is a nonessential amino acid, meaning it can be manufactured by the human body, and does not need to be obtained through the diet. Alanine is found in a wide ...
It is a conditionally essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. [3] [4] It is called tyrosyl when referred to as a functional group or side chain.
Glycocyamine (or guanidinoacetate) is a metabolite of glycine in which the amino group has been converted into a guanidine by guanylation (transfer of a guanidine group from arginine). In vertebrate organism it is then transformed into creatine by methylation. Glycocyamine is used as a supplement and as a feed additive in poultry farming.
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.