Control of lysyl oxidase activity through site-specific deuteration of lysine.

@article{Pestov2011ControlOL,
  title={Control of lysyl oxidase activity through site-specific deuteration of lysine.},
  author={Nikolay B. Pestov and Irina A. Okkelman and Vadim V Shmanai and Alaksiej L Hurski and Amato J. Giaccia and Mikhail S Shchepinov},
  journal={Bioorganic & medicinal chemistry letters},
  year={2011},
  volume={21 1},
  pages={255-8}
}
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… CONTINUE READING