L-Lysine

L-lysine is an essential amino acid for humans and therefore must be supplied in the diet. lysine's popularity as a nutritional supplement arose as a result of some studies suggesting that the amino acid may decrease the recurrence rate of some infected with herpes simplex virus.

Lysine deficiencies may include fatigue, moodiness, anemia, poor concentration, reproductive problems and slow development. L-Lysine supplementation helps maintain the health of the structural, circulatory and immune systems. For years, lysine has been considered in the treatment of herpes and cold sores, and more recently, has been attracting attention as a possible addition to the fast-growing list of muscle-building nutrients.

Natural Food Sources For L-Lysine :

Certain proteins, such as those found in meat, poultry and milk are rich in L-lysine. Proteins found in grains, cereals and their products are typically low in L-lysine. For example, wheat is low in L-lysine; wheat germ, however, is rich in L-lysine. Small amounts of free L-lysine are found in vegetables, vegetable juices and in such fermented foods as miso and yogurt.

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( L-Lysine )

Lysine (abbreviated as Lys or K)^[1] is an α-amino acid with the chemical formula HO₂CCH(NH₂)(CH₂)₄NH₂. 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 often participates in hydrogen bonding and as 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.

Biosynthesis

As an essential amino acid, lysine is not synthesized in animals, hence it must be ingested as lysine or lysine-containing proteins. In plants and microorganisms, it is synthesized from aspartic acid, which is first converted to β-aspartyl-semialdehyde. Cyclization gives dihydropicolinate, which is reduced to Δ¹-piperidine-2,6-dicarboxylate. Ring-opening of this heterocycle gives a series of derivatives of pimelic acid, ultimately affording lysine. Enzymes involved in this biosynthesis include:^[2]

Reference:

http://en.wikipedia.org/wiki/Lysine