| Compound Description | L-lysine is an L-alpha-amino acid; the L-isomer of lysine. It has a role as a micronutrient, a nutraceutical, an anticonvulsant, an Escherichia coli metabolite, a Saccharomyces cerevisiae metabolite, a plant metabolite, a human metabolite, an algal metabolite and a mouse metabolite. It is an aspartate family amino acid, a proteinogenic amino acid, a lysine and a L-alpha-amino acid. It is a conjugate base of a L-lysinium. It is a conjugate acid of a L-lysinate. It is an enantiomer of a D-lysine. It is a tautomer of a L-lysine zwitterion and a L-Lysine zwitterion.Lysine is an α-amino acid with the chemical formula HO2CCH4NH2. This amino acid is an essential amino acid, which means that humans cannot synthesize it. Its codons are AAA and AAG. Lysine is a base, as are arginine and histidine. The ε-amino group acts as a site for hydrogen binding and a general base in catalysis. Common posttranslational modifications include methylation of the ε-amino group, giving methyl-, dimethyl-, and trimethyllysine. The latter occurs in calmodulin. Other posttranslational modifications include acetylation. Collagen contains hydroxylysine which is derived from lysine by lysyl hydroxylase. O-Glycosylation of lysine residues in the endoplasmic reticulum or Golgi apparatus is used to mark certain proteins for secretion from the cell.L-Lysine is a metabolite found in or produced by Escherichia coli .Lysine is a natural product found in Pinus densiflora, Cyperus aromaticus, and other organisms with data available.Lysine is one of nine essential amino acids in humans required for growth and tissue repair, Lysine is supplied by many foods, especially red meats, fish, and dairy products. Lysine seems to be active against herpes simplex viruses and present in many forms of diet supplements. The mechanism underlying this effect is based on the viral need for amino acid arginine; lysine competes with arginine for absorption and entry into cells. Lysine inhibits HSV growth by knocking out arginine. L-Lysine is an alpha-amino acid with the chemical formula HO2CCH4NH2. This amino acid is an essential amino acid, which means that humans cannot synthesize it. Its codons are AAA and AAG.
L-Lysine is a base, as are arginine and histidine. The epsilon-amino group often participates in hydrogen bonding and as a general base in catalysis. Common posttranslational modifications include methylation of the epsilon-amino group, giving methyl-, dimethyl-, and trimethyllysine. The latter occurs in calmodulin. Other posttranslational modifications include acetylation. Collagen contains hydroxylysine which is derived from lysine by lysyl hydroxylase. O-Glycosylation of lysine residues in the endoplasmic reticulum or Golgi apparatus is used to mark certain proteins for secretion from the cell.L-lysine is an essential amino acid. Normal requirements for lysine have been found to be about 8 g per day or 12 mg/kg in adults. Children and infants need more- 44 mg/kg per day for an eleven to-twelve-year old, and 97 mg/kg per day for three-to six-month old. Lysine is highly concentrated in muscle compared to most other amino acids. Lysine is high in foods such as wheat germ, cottage cheese and chicken. Of meat products, wild game and pork have the highest concentration of lysine. Fruits and vegetables contain little lysine, except avocados. Normal lysine metabolism is dependent upon many nutrients including niacin, vitamin B6, riboflavin, vitamin C, glutamic acid and iron. Excess arginine antagonizes lysine. Several inborn errors of lysine metabolism are known. Most are marked by mental retardation with occasional diverse symptoms such as absence of secondary sex characteristics, undescended testes, abnormal facial structure, anemia, obesity, enlarged liver and spleen, and eye muscle imbalance. Lysine also may be a useful adjunct in the treatment of osteoporosis. Although high protein diets result in loss of large amounts of calcium in urine, so does lysine deficiency. Lysine may be an adjunct therapy because it reduces calcium losses in urine. Lysine deficiency also may result in immunodeficiency. Requirements for this amino acid are probably increased by stress. Lysine toxicity has not occurred with oral doses in humans. Lysine dosages are presently too small and may fail to reach the concentrations necessary to prove potential therapeutic applications. Lysine metabolites, amino caproic acid and carnitine have already shown their therapeutic potential. Thirty grams daily of amino caproic acid has been used as an initial daily dose in treating blood clotting disorders, indicating that the proper doses of lysine, its precursor, have yet to be used in medicine. Low lysine levels have been found in patients with Parkinson's, hypothyroidism, kidney disease, asthma and depression. The exact significance of these levels is unclear, yet lysine therapy can normalize the level and has been associated with improvement of some patients with these conditions. Abnormally elevated hydroxylysines have been found in virtually all chronic degenerative diseases and coumadin therapy. The levels of this stress marker may be improved by high doses of vitamin C. Lysine is particularly useful in therapy for marasmus and herpes simplex. It stops the growth of herpes simplex in culture, and has helped to reduce the number and occurrence of cold sores in clinical studies. Dosing has not been adequately studied, but beneficial clinical effects occur in doses ranging from 100 mg to 4 g a day. Higher doses may also be useful, and toxicity has not been reported in doses as high as 8 g per day. Diets high in lysine and low in arginine can be useful in the prevention and treatment of herpes. Some researchers think herpes simplex virus is involved in many other diseases related to cranial nerves such as migraines, Bell's palsy and Meniere's disease. Herpes blister fluid will produce fatal encephalitis in the rabbit.An essential amino acid. It is often added to animal feed.See also: Lysine Hydrochloride ; Glatiramer Acetate ; Glatiramer ... View More ... |
