β-Lysine

β-Lysine
Names
IUPAC name
3,6-Diaminohexanoic acid
Identifiers
3D model (JSmol)
ChemSpider
UNII
  • InChI=1S/C6H14N2O2/c7-3-1-2-5(8)4-6(9)10/h5H,1-4,7-8H2,(H,9,10) checkY
    Key: QKEWQOJCHPFEAF-UHFFFAOYSA-N checkY
  • InChI=1/C6H14N2O2/c7-3-1-2-5(8)4-6(9)10/h5H,1-4,7-8H2,(H,9,10)
    Key: QKEWQOJCHPFEAF-UHFFFAOYAC
  • C(CC(CC(=O)O)N)CN
Properties
C6H14N2O2
Molar mass 146.190 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

β-Lysine (3,6-diaminohexanoic acid[1]) is an amino acid produced by platelets during coagulation and is directly antibacterial by causing lysis of many Gram positive bacteria by acting as a cationic detergent.[2] Beta Lysine contains a side chain with an amino group and is the beta form of the amino acid Lysine. Beta-Lysine can hydrogen bond at its carboxylic acid residue.[3] Lysine is an amino acid that acts as a site for ubiquitination enzymes to bind to and branch from.[4] Lysine is a positively charged amino acid due to its amino side chain (that contains an amine). This allows Beta-Lysine to directly interact with the negatively charged phosphate groups within nucleotides.[4]

Beta-lysine is a non-specific immune defense factor that can be found in the blood of many animals, including birds this contributes to the innate immune system.[5] Beta-Lysine in turn, can be a form of measure, of overall immune activity.[5] Beta-Lysine activity is also responsive to many immunomodulators, such as preparations containing bacterial lipopolysaccharides, which increase the musical immune response which then leads to an increase in Beta-Lysine activity, further solidifying Beta-Lysine as an indicator and form of measure for innate immune response.

References

  1. ↑ "beta-lysine". curehunter.com. Retrieved 2010-04-18.
  2. ↑ Mayer, Gene. "Immunology – Chapter One > Innate (Non-Specific) Immunity". University of South Carolina. Immunology Section of Microbiology and Immunology On-line.
  3. ↑ Li, Hai; Govorunova, Elena G.; Sineshchekov, Oleg A.; Spudich, John L. (April 2014). "Role of a Helix B Lysine Residue in the Photoactive Site in Channelrhodopsins". Biophysical Journal. 106 (8): 1607–1617. doi:10.1016/j.bpj.2014.03.002. PMC 4008836. PMID 24739160.
  4. 1 2 Jang, Eun Jung; Park, Hye Ryeon; Hong, Jeong-Ho; Hwang, Eun Sook (2013-06-01). "Lysine 313 of T-box Is Crucial for Modulation of Protein Stability, DNA Binding, and Threonine Phosphorylation of T-bet". The Journal of Immunology. 190 (11): 5764–5770. doi:10.4049/jimmunol.1203403. ISSN 0022-1767. PMID 23616576.
  5. 1 2 Karakolev, Rumen; Petrova-Tsenın, Preslava; Petrova, Reneta; Koynarskı, Tsvetoslav (2022-06-30). "Effect of Avigen immunomodulator on beta lysine activity in broilers". Yuzuncu Yıl University Journal of Agricultural Sciences. 32 (2): 260–265. doi:10.29133/yyutbd.1013030. ISSN 1308-7576.


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