Linked from

The 12 pages that link to Lysine, each with the reason it gives.

• Maillard reactionRelated: Its amino group can be modified during processing, reducing the nutritional availability of lysine.

• AcetylationRelated: Its side-chain amino group is a frequent protein acetylation site.

• Tranexamic acidRelated: Tranexamic acid is a synthetic lysine analogue that competes for plasminogen-binding sites.

• Ubiquitin–proteasome systemRelated: Ubiquitin commonly attaches to lysine residues on substrate proteins.

• UbiquitinRelated: Ubiquitin chains often link through lysine residues.

• SeitanRelated: Seitan’s low lysine content can be balanced with lysine-rich foods such as legumes.

• LeucineCompared with: Like leucine, lysine is exclusively ketogenic, but its structure and cellular roles differ.

• ArginineCompared with: Like arginine, lysine is basic, but it is essential and lacks arginine’s guanidinium group.

• HistidineCompared with: Unlike histidine’s imidazole, lysine’s side chain is usually positively charged under physiological conditions.

• BiotinRelated: Biotin is covalently attached to a lysine residue in biotin-dependent enzymes.

• Glutaric acidRelated: Lysine degradation can generate glutaric acid as an intermediate.

• CadaverineBroader topic: Bacterial decarboxylation of this amino acid yields cadaverine.