Allysine

Last updated
Allysine
Allysine.svg
L-Allysine-zwitterion-3D-balls.png
Names
Preferred IUPAC name
(2S)-2-Amino-6-oxohexanoic acid
Other names
2-aminoadipate semialdehyde, 2-amino-5-formylvaleric acid, norvaline, 6-oxo-DL-norleucine
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
KEGG
MeSH allysine
PubChem CID
UNII
  • InChI=1S/C6H11NO3/c7-5(6(9)10)3-1-2-4-8/h4-5H,1-3,7H2,(H,9,10) Yes check.svgY
    Key: GFXYTQPNNXGICT-UHFFFAOYSA-N Yes check.svgY
  • InChI=1/C6H11NO3/c7-5(6(9)10)3-1-2-4-8/h4-5H,1-3,7H2,(H,9,10)/t5-/m0/s1
    Key: GFXYTQPNNXGICT-YFKPBYRVBJ
  • InChI=1/C6H11NO3/c7-5(6(9)10)3-1-2-4-8/h4-5H,1-3,7H2,(H,9,10)
    Key: GFXYTQPNNXGICT-UHFFFAOYAD
  • O=CCCC[C@H](N)C(=O)O
  • O=CCCCC(N)C(=O)O
Properties
C6H11NO3
Molar mass 145.158 g·mol−1
Appearanceunstable
Density 1.74g/cm3
Boiling point 295.2 °C (563.4 °F; 568.3 K)
Hazards
Flash point 132.3 °C (270.1 °F; 405.4 K)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
X mark.svgN  verify  (what is  Yes check.svgYX mark.svgN ?)

Allysine is a derivative of lysine that features a formyl group in place of the terminal amine. The free amino acid does not exist, but the allysine residue does. It is produced by aerobic oxidation of lysine residues by the enzyme lysyl oxidase. The transformation is an example of a post-translational modification. The semialdehyde form exists in equilibrium with a cyclic derivative. [1]

Contents

Conversion of lysine residue to allysine residue. PTMofLysine.svg
Conversion of lysine residue to allysine residue.

Allysine is involved in the production of elastin and collagen. [2] Increased allysine concentration in tissues has been correlated to the presence of fibrosis. [3]

Allysine residues react with sodium 2-naphthol-6-sulfonate to produce a fluorescent bis-naphtol-allysine product. [4] In another assay, allysine-containing proteins are reduced with sodium borohydride to give a peptide containing the 6-hydroxynorleucine (6-hydroxy-2-aminocaproic acid) residue, which (unlike allysine) is stable to proteolysis. [1]

Further reading

See also

References

  1. 1 2 Requena, J. R.; Levine, R. L.; Stadtman, E. R. (2003). "Recent Advances in the Analysis of Oxidized Proteins". Amino Acids. 25 (3–4): 221–226. doi:10.1007/s00726-003-0012-1. PMID   14661085. S2CID   28837698.
  2. ↑ Eyre, David R.; Paz, Mercedes A.; Gallop, Paul M. (1984). "Cross-Linking in Collagen and Elastin". Annual Review of Biochemistry. 53: 717–748. doi:10.1146/annurev.bi.53.070184.003441. PMID   6148038.
  3. ↑ Wahsner J, Désogère P, Abston E, Graham-O'Regan KA, Wang J, Rotile NJ, et al. (April 2019). "68Ga-NODAGA-Indole: An Allysine-Reactive Positron Emission Tomography Probe for Molecular Imaging of Pulmonary Fibrogenesis". Journal of the American Chemical Society. 141 (14): 5593–5596. doi:10.1021/jacs.8b12342. PMC   6494104 . PMID   30908032.
  4. ↑ Waghorn PA, Oliveira BL, Jones CM, Tager AM, Caravan P (October 2017). "High sensitivity HPLC method for determination of the allysine concentration in tissue by use of a naphthol derivative". Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences. 1064: 7–13. doi:10.1016/j.jchromb.2017.08.032. PMC   5662445 . PMID   28886479.


This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.