Structure via PubChem · Public domain (PubChem)
allysine
Sign in to saveAlso known as HCO-[CH2]3-CH(NH2)-COOH, alpha-aminoadipic delta-semialdehyde, alpha-aminoadipic acid delta-semialdehyde, 6-oxonorleucine, 2-amino-5-formylvaleric acid, DL-allysine
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. thumb|center|Conversion of lysine residue to allysine residue.|380px
Chemical data
- Formula
- C6H11NO3
- Molecular weight
- 145.16 g/mol
- IUPAC name
- 2-amino-6-oxohexanoic acid
- SMILES
- C(CC=O)CC(C(=O)O)N
- InChIKey
- GFXYTQPNNXGICT-UHFFFAOYSA-N
- XLogP
- -3.2
- Polar surface area
- 80.4 Ų
- H-bond donors
- 2
- H-bond acceptors
- 4
- Formal charge
- 0
via PubChem
Wikidata facts
- Subclass of
- primary metabolite
- Mass
- 145.073893
Show 4 more facts
- chemical formula
- C₆H₁₁NO₃
- canonical SMILES
- C(CC=O)CC(C(=O)O)N
- Commons category
- Allysine
- found in taxon
- Caenorhabditis elegans
via Wikidata · CC0
~1 min read
Encyclopedic overview
3 sectionsContents
- Biochemical reactions
- References
- Further reading
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. thumb|center|Conversion of lysine residue to allysine residue.|380px
==Biochemical reactions== Allysine is linked to L-lysine in reactions catalysed by saccharopine dehydrogenases. These interconvert them via saccharopine:
Excerpted from Wikipedia’s “allysine” article, available under the CC BY-SA 4.0 licence.