Acetyllysine

Acetyllysine (or acetylated lysine) is an acetyl-derivative of the amino acid lysine. There are multiple forms of acetyllysine: this article is about N-ε-acetyl-L-lysine; the other form is N-α-acetyl-L-lysine.

Acetyllysine
Skeletal formula of acetyllysine (S)
Names
Other names
  • 6-Acetamido-2-aminohexanoic acid
  • 2-Azaniumyl-6-acetamidohexanoate
Identifiers
3D model (JSmol)
1725438 S
ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.010.661
EC Number
  • 211-725-9
747339 S
KEGG
MeSH N-epsilon-acetyllysine
UNII
  • InChI=1S/C8H16N2O3/c1-6(11)10-5-3-2-4-7(9)8(12)13/h7H,2-5,9H2,1H3,(H,10,11)(H,12,13) ☒N
    Key: DTERQYGMUDWYAZ-UHFFFAOYSA-N ☒N
  • CC(=O)NCCCC[C@H](N)C(=O)O
Properties
C8H16N2O3
Molar mass 188.227 g·mol−1
Appearance White crystals
Odor Odourless
Density 1.139 g/mL
Melting point 250 °C (482 °F; 523 K)
Boiling point 442 °C (828 °F; 715 K)
log P −0.961
Acidity (pKa) 2.529
Basicity (pKb) 11.468
Related compounds
Related alkanoic acids
 Pivagabine
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

In proteins, the acetylation of lysine residues is an important mechanism of epigenetics. It functions by regulating the binding of histones to DNA in nucleosomes and thereby controlling the expression of genes on that DNA. Non-histone proteins are acetylated as well. Unlike the functionally similar methyllysine, acetyllysine does not carry a positive charge on its side chain.

Histone acetyltransferases (HATs) catalyze the addition of acetyl groups from acetyl-CoA onto certain lysine residues of histones and non-histone proteins. Histone deacetylases (HDACs) catalyze the removal of acetyl groups from acetylated lysines.

Acetyllysine can be synthesized from lysine by the selective acetylation of the terminal amine group.[1]

References
  1. For example: Kikugawa, Mitsui, Sakamoto (1990). "N-methoxydiacetamide: A new selective acetylating agent". Journal Tetrahedron Letters. 31 (2): 243–246. doi:10.1016/S0040-4039(00)94382-X.
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