Lysine residues of basic strength (pKa about 10.5) is weak in arginine. Fat tetramethylene group is hydrophobic, but proton dominator hydrophilic amine groups. When you carry a positive charge, the lysine residues provide a negative charge and bond positions, often contain strong hydrogen bonds. In vivo, lysine and hydroxyl lysine is to maintain three strands of collagen peptides have more than the required stability. Chemical reaction side chain include activated esters and acid anhydride acylation reaction (acylation) and modification aldehyde, imidate esters and the isocyanate. Lysine (English: Lysine referred to as Lys or K) is an α- amino acid. Its chemical formula is expressed as: HO2CCH (NH2) (CH2) 4NH2. Lysine is an essential amino acid. Lysine genetic code is AAA and AAG.
Lysine and arginine, histidine, as part of the basic amino acids. ε- amino group involved in the synthesis of hydrogen bonds and often play the role of universal bases in the catalytic reactions. (Ε- amino group (NH3 +) and fifth carbon atoms starting from the α- carbon attached; α- carbon is carboxy (C = OOH) bonded to carbon atoms.)
Ε- amino group of lysine methylation is a post-translational modification generally, the formation of a methyl, dimethyl and trimethyl lysine. Trimethyl-lysine will happen in calmodulin. In addition, the lysine residues but also for acetylation and ubiquitination and other modifications. Hydroxy lysine contains collagen by lysine hydroxylation by lysine hydroxylase from. The ER or Golgi, O- sugar hydroxy lysine residues glycosylated proteins can be used to mark specific secreted from the cell.
Lysine can be two stereo isomeric L- or D- form of presence. But only L- type present in a biological proteins. D- amino acid can be converted into L- type amino acids. D- lysine no biological activity, therefore, all the commercial production of lysine are L- lysine type.