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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.
These six are arginine, cysteine, glycine, glutamine, proline, and tyrosine. Six amino acids are non-essential (dispensable) in humans, meaning they can be synthesized in sufficient quantities in the body. These six are alanine, aspartic acid, asparagine, glutamic acid, serine, [2] and selenocysteine (considered the 21st amino acid).
Arginine and proline metabolism is one of the central pathways for the biosynthesis of the amino acids arginine and proline from glutamate. The pathways linking arginine, glutamate, and proline are bidirectional. Thus, the net utilization or production of these amino acids is highly dependent on cell type and developmental stage.
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
For example, lysine and arginine are present in large amounts in the low-complexity regions of nucleic-acid binding proteins. [40] There are various hydrophobicity scales of amino acid residues. [41] Some amino acids have special properties. Cysteine can form covalent disulfide bonds to other cysteine residues.
Argininemia is an autosomal recessive urea cycle disorder where a deficiency of the enzyme arginase causes a buildup of arginine and ammonia in the blood.Ammonia, which is formed when proteins are broken down in the body, is toxic if levels become too high; the nervous system is especially sensitive to the effects of excess ammonia.
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