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Lysine

C6H14N2O2 organic

Properties

StateSolid (white crystalline powder)
ColorWhite
SolubilityHighly soluble in water (freely soluble); slightly soluble in ethanol
Melting Point224 °C (decomposes)
Boiling PointDecomposes before boiling

About Lysine

Lysine, three-letter Lys and one-letter K, is the amino acid whose side chain is a four-carbon tether ending in a primary amine. The side-chain pKa sits around 10.5, so at physiological pH the epsilon-NH3+ carries a full positive charge — and that single feature drives most of what lysine does in biology. Histone tails are Lys-rich precisely because that string of cations grips the phosphate backbone of DNA; flip those Lys side chains from charged to acetylated (HDAC and HAT enzymes do this dynamically) and the chromatin loosens, transcription opens up. Methylation at H3K4 versus H3K9 versus H3K27 means completely different things to a cell, and reading those marks is the day job of bromodomain and chromodomain proteins. In collagen, lysyl oxidase oxidatively deaminates specific Lys and hydroxylysine residues to allysine; the resulting aldehydes then condense into the trivalent cross-links that give skin and tendon their tensile strength — defective lysyl oxidase is what makes a copper-deficient diet produce floppy connective tissue. Lysine also matters at the dinner table: it is the first limiting amino acid in wheat, rice, and corn, which is why the rice-and-beans, wheat-and-lentils, corn-and-bean pairings that emerged independently across cultures all hit the same biochemical target. Industrially, L-lysine is fermented from glucose by Corynebacterium glutamicum at megaton scale for animal feed.

Where you'll encounter it

If you have ever supplemented a vegetarian diet with legumes, fed a pig or chicken on a corn-based ration, or pulled a Western blot probing for an acetyl-K mark on histone H3, you have been working with lysine biochemistry directly. Swine and poultry nutritionists run feed formulations on a 'standardized ileal digestible lysine' basis precisely because Lys is the first limiting amino acid in corn and soybean rations — drop synthetic L-lysine HCl by 0.1% and growth rate stalls within a week. Epigenetics researchers ordering H3K9me3 or H3K27ac antibodies from Cell Signaling are buying reagents that distinguish methyl from acetyl marks on the same Lys residue, and the choice between H3K4me3 (active promoter) and H3K9me3 (heterochromatin) drives the entire interpretation of a ChIP-seq experiment.

Common Uses

  • Animal-feed supplement (L-lysine HCl), produced at roughly 2.5 million tonnes per year by C. glutamicum fermentation
  • Essential dietary amino acid, first limiting in wheat, rice, and corn
  • Substrate for histone acetylation and methylation marks studied in epigenetics
  • Substrate for lysyl oxidase in collagen and elastin cross-link formation
  • L-lysine HCl supplements (1-3 g/day) marketed for cold-sore prophylaxis
  • Building block in solid-phase peptide synthesis using Fmoc-Lys(Boc)-OH

Safety Information

GRAS for food and feed use. Free L-lysine and L-lysine HCl are well tolerated at supplementation doses of 1 to 3 g per day; gram-scale boluses can produce GI cramping or osmotic diarrhea. Sustained intakes above roughly 6 g/day have been linked to reduced renal arginine reabsorption in case reports. Not classified under GHS. The DL-mixture and the unnatural D-enantiomer have no nutritional value and should not be used in feed.

This safety summary is for educational reference only and may not be complete. It is not a substitute for Safety Data Sheets (SDS), medical advice, or professional chemical safety guidance. Always consult appropriate SDS and qualified professionals before handling chemicals.

Constituent Elements

Frequently Asked Questions

What is the molar mass of lysine?
Free-base L-lysine (C6H14N2O2) is 146.188 g/mol: 6 C (72.066) + 14 H (14.112) + 2 N (28.014) + 2 O (31.998). The commercial monohydrochloride form L-Lys HCl that ships in feed bags is 182.65 g/mol.
Why does lysine matter so much in epigenetics?
The epsilon-amine on lysine is a uniquely tunable post-translational handle. HATs add an acetyl group, neutralizing the positive charge and weakening histone-DNA contact. HDACs strip it back off. Lysine methyltransferases write mono-, di-, or trimethyl marks without changing charge but creating distinct binding sites for chromodomain readers. The same residue (e.g., H3K9) can mean active or repressed transcription depending on which mark is present, and small-molecule HDAC and BET inhibitors are now FDA-approved cancer drugs.
Why are cereal grains low in lysine?
The bulk storage proteins in cereals — zein in maize, gliadin in wheat, kafirins in sorghum — are prolamins that evolved to be nitrogen-dense storage depots, heavy in glutamine and proline and naturally low in lysine and tryptophan. Pairing grains with legume seed-storage proteins (which are lysine-rich but methionine-poor) recovers the missing residues, which is the biochemistry behind every grain-and-bean staple cuisine.