A structure-activity study to identify novel and efficient substrates of the human semicarbazide-sensitive amine oxidase/VAP-1 enzyme.

@article{Bonaiuto2010ASS,
  title={A structure-activity study to identify novel and efficient substrates of the human semicarbazide-sensitive amine oxidase/VAP-1 enzyme.},
  author={E. Bonaiuto and M. Lunelli and Marina Scarpa and R. Vettor and G. Milan and M. D. Di Paolo},
  journal={Biochimie},
  year={2010},
  volume={92 7},
  pages={
          858-68
        }
}
  • E. Bonaiuto, M. Lunelli, +3 authors M. D. Di Paolo
  • Published 2010
  • Medicine, Chemistry
  • Biochimie
  • Kinetic studies were performed with various alkanamines as "substrate probes" of the properties of the active site of the human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO/VAP-1). We found that the enzyme-substrate recognition step is mainly controlled by apolar interactions and that a "good" substrate has a molecular structure containing a long aliphatic chain and a second positive charge at a distance greater than 12 A from the reactive amino group. In this context… CONTINUE READING
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