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Histidine. Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Histidine (symbol His or H) [2] is an essential amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated –NH 3+ form under biological conditions), a carboxylic ...
Animals obtain aromatic amino acids from their diet, but nearly [a] all plants and some micro-organisms must synthesize their aromatic amino acids through the metabolically costly shikimate pathway in order to make them. Histidine, phenylalanine, tryptophan, are essential amino acids for animals. Since they are not synthesized in the human body ...
Amino acid biosynthesis is the set of biochemical processes (metabolic pathways) by which the amino acids are produced. The substrates for these processes are various compounds in the organism 's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids.
Amino acid. Structure of a typical L -alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2]
Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation. 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) that can ...
Essential amino acid. An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are valine, isoleucine ...
Heterocycles are often activated towards cation–π binding when the lone pair on the heteroatom is in incorporated into the aromatic system (e.g. indole, pyrrole). Conversely, when the lone pair does not contribute to aromaticity (e.g. pyridine), the electronegativity of the heteroatom wins out and weakens the cation–π binding ability.
Histidine decarboxylase is a group II pyridoxal-dependent decarboxylase, along with aromatic-L-amino-acid decarboxylase, and tyrosine decarboxylase. HDC is expressed as a 74 kDa polypeptide which is not enzymatically functional. [7][8] Only after post-translational processing does the enzyme become active.