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Lysine. Technically, any organic compound with an amine (–NH 2) and a carboxylic acid (–COOH) functional group is an amino acid. The proteinogenic amino acids are a small subset of this group that possess a central carbon atom (α- or 2-) bearing an amino group, a carboxyl group, a side chain and an α-hydrogen levo conformation, with the exception of glycine, which is achiral, and proline ...
The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. 2-Aminothiazoline-4-carboxylic acid is an intermediate in the industrial synthesis of L-cysteine for example.
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] Only these 22 appear in the genetic code of life ...
Ribosomes translate the codons to their respective amino acids. [1] In humans, non-essential amino acids are synthesized from intermediates in major metabolic pathways such as the Citric Acid Cycle. [2] Essential amino acids must be consumed and are made in other organisms. The amino acids are joined by peptide bonds making a polypeptide chain.
Serine (symbol Ser or S) [3] [4] is an α-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 carboxyl group (which is in the deprotonated − COO −
Glutamine is the most abundant naturally occurring, nonessential amino acid in the human body, and one of the few amino acids that can directly cross the blood–brain barrier. [7] Humans obtain glutamine through catabolism of proteins in foods they eat. [ 23 ]
Transamination is a chemical reaction that transfers an amino group to a ketoacid to form new amino acids.This pathway is responsible for the deamination of most amino acids. This is one of the major degradation pathways which convert essential amino acids to non-essential amino acids (amino acids that can be synthesized de novo by the organism).
The different amino acids are identified by the functional group. As a result of the three different groups attached to the α-carbon, amino acids are asymmetrical molecules. For all standard amino acids, except glycine, the α-carbon is a chiral center. In the case of glycine, the α-carbon has two hydrogen atoms, thus adding symmetry to this ...