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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 ...
Glutamine provides a source of carbon and nitrogen for use in other metabolic processes. Glutamine is present in serum at higher concentrations than other amino acids [16] and is essential for many cellular functions. Examples include the synthesis of nucleotides and non-essential amino acids. [17]
It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG). Proline is the only proteinogenic amino acid which is a secondary amine , as the nitrogen atom is attached both to the α-carbon and to a chain of three ...
3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain carboxamide, classifying it as a polar (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it. It is encoded by the codons AAU and AAC.
The synthesis of essential amino acids such as are L-Methionine, L-Lysine, L-Tryptophan and the non-essential amino acid L-Glutamic acid are used today mainly for feed, food, and pharmaceutical industries. The production of these amino acids is due to Corynebacterium glutamicum and fermentation.
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.
Aspartic acid has an acidic side chain (CH 2 COOH) which reacts with other amino acids, enzymes and proteins in the body. [5] Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged aspartate form, −COO −. [5] It is a non-essential amino acid in humans, meaning the body can synthesize it as
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.
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