Of or pertaining to lysine:
Lysine (symbol Lys or K) is an α-amino acid that is a precursor to many proteins.
It contains an α-amino group (which is in the protonated −NH+3 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 basic, charged (at physiological pH), aliphatic amino acid.
Lysyl oxidase (LOX), also known as protein-lysine 6-oxidase, is an enzyme that, in humans, is encoded by the LOX gene.
It catalyzes the conversion of lysine residues into its aldehyde derivative allysine.
Allysine form cross-links in extracellular matrix proteins.
Inhibition of lysyl oxidase can cause osteolathyrism, but, at the same time, its upregulation by tumor cells may promote metastasis of the existing tumor, causing it to become malignant and cancerous.
Lysyl hydroxylases (or procollagen-lysine 5-dioxygenases) are alpha-ketoglutarate-dependent hydroxylases enzymes that catalyze the hydroxylation of lysine to hydroxylysine.
Lysyl hydroxylases require iron and vitamin C as cofactors for their oxidation activity.
It takes place (as a post-translational modification) following collagen synthesis in the cisternae (lumen) of the rough endoplasmic reticulum (ER).
Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase, and caseinase) is an enzyme.
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Photo: Pixabay/GDJ
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