Lysine degradation

Lysine

Skeletal formula of the L-monocation (positive polar form)

Ball-and-stick model of lysine at physiological pH (zwitterionic form)

Names

IUPAC name

Lysine

Other names

2,6-Diaminohexanoic acid; 2,6-Diammoniohexanoic acid

Identifiers

CAS Number

70-54-2 DL^N
56-87-1 L^Y
923-27-3 D^Y

3D model (Jmol)

Interactive image

ChEBI

CHEBI:25094^Y

ChemSpider

843^Y
5747 L^Y

C16440^N

PubChem CID

UNII

K3Z4F929H6^Y

InChI

InChI=1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)^Y

Key: KDXKERNSBIXSRK-UHFFFAOYSA-N^Y
InChI=1/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)

Key: KDXKERNSBIXSRK-UHFFFAOYAY

SMILES

C(CCN)CC(C(=O)O)N

Properties

Chemical formula

C₆H₁₄N₂O₂

Molar mass

146.19 g·mol⁻¹

Solubility in water

1.5kg/L @ 25 °C

Pharmacology

ATC code

B05XB03 (WHO)

Supplementary data page

Structure and
properties

Refractive index (n),
Dielectric constant (ε_r), etc.

Thermodynamic
data

Phase behaviour
solid–liquid–gas

Spectral data

UV, IR, NMR, MS

Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

(what is ^YN ?)

Infobox references

Lysine (abbreviated as Lys or K), encoded by the codons AAA and AAG, is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH₃⁺ form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO⁻ form under biological conditions), and a side chain lysyl ((CH₂)₄NH₂), classifying it as a charged (at physiological pH), aliphatic amino acid. It is essential in humans, meaning the body cannot synthesize it and thus it must be obtained from the diet.

Lysine is a base, as are arginine and histidine. The ε-amino group often participates in hydrogen bonding and as a general base in catalysis. The ε-amino group (NH₃⁺) is attached to the fifth carbon from the α-carbon, which is attached to the carboxyl (C=OOH) group.

Common posttranslational modifications include methylation of the ε-amino group, giving methyl-, dimethyl-, and trimethyllysine (the latter occurring in calmodulin); also acetylation, sumoylation, ubiquitination, and hydroxylation - producing the hydroxylysine in collagen and other proteins. O-Glycosylation of hydroxylysine residues in the endoplasmic reticulum or Golgi apparatus is used to mark certain proteins for secretion from the cell. In opsins like rhodopsin and the visual opsins (encoded by the genes OPN1SW, OPN1MW, and OPN1LW), retinaldehyde forms a Schiff base with a conserved lysine residue, and interaction of light with the retinylidene group causes signal transduction in color vision (See visual cycle for details). Deficiencies may cause blindness, as well as many other problems due to its ubiquitous presence in proteins.

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Wikipedia