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Lysyl oxidase (LOX) is implicated in several extracellular matrix related disorders, including fibrosis and cancer. Methods of inhibition of LOX in vivo include antibodies, copper sequestration and toxic small molecules such as β-aminopropionitrile. Here, we propose a novel approach to modulation of LOX activity based on the kinetic isotope effect (KIE). We show that 6,6-d(2)-lysine is oxidised by LOX at substantially lower rate, with apparent deuterium effect on V(max)/K(m) as high as 4.35 ± 0.22. Lys is an essential nutrient, so dietary ingestion of D(2)Lys and its incorporation via normal Lys turnover suggests new approaches to mitigating LOX-associated pathologies.

Original publication




Journal article


Bioorg Med Chem Lett

Publication Date





255 - 258


Animals, Deuterium, Isotope Labeling, Kinetics, Lysine, Mice, Oxidation-Reduction, Protein-Lysine 6-Oxidase, Recombinant Proteins, Sheep, Substrate Specificity