Identification of a Novel SubstrateDerived Spermine Oxidase Inhibitor

T. T. Dunston, M. A. Khomutov, S. B. Gabelli, T. M. Stewart, J. R. Foley, S. N. Kochetkov, A. R. Khomutov, R. A. Casero

Research output: Contribution to journalArticlepeer-review


Homeostasis of the biogenic polyamines spermine (Spm) and spermidine (Spd), present in μM-mM concentrations in all eukaryotic cells, is precisely regulated by coordinated activities of the enzymes of polyamine synthesis, degradation, and transport, in order to sustain normal cell growth and viability. Spermine oxidase (SMOX) is the key and most recently discovered enzyme of polyamine metabolism that plays an essential role in regulating polyamine homeostasis by catalyzing the back-conversion of Spm to Spd. The development of many types of epithelial cancer is associated with inflammation, and disease-related inflammatory stimuli induce SMOX. MDL72527 is widely used in vitro and in vivo as an irreversible inhibitor of SMOX, but it is also potent towards N1 -acetylpolyamine oxidase. Although SMOX has high substrate specificity, Spm analogues have not been systematically studied as enzyme inhibitors.

Original languageEnglish (US)
Pages (from-to)140-144
Number of pages5
JournalActa Naturae
Issue number3
StatePublished - 2020


  • 2,11-Met2-Spm
  • MDL72527
  • Spermine oxidase
  • inhibitors
  • spermine analogues

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology


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