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Gene Review

PAOX  -  polyamine oxidase (exo-N4-amino)

Bos taurus

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Disease relevance of PAOX

  • The physiological importance of polyamine oxidase mediated trypanolysis is unclear; even at peak parasitemia in cattle (10(7) organisms/ml) it can be calculated that trypanosomes would not release enough spermidine for the generation of sufficient quantities of toxic degradation products [1].

High impact information on PAOX

  • Oxidation of the biologically important polyamines spermine and spermidine by plasma amine oxidase (PAO) was specified many years ago to occur at the terminal primary rather than internal secondary amine positions [2].
  • We further find no evidence for the ability of PAO to metabolize the secondary amine position in homospermidine, which is devoid of such complicating side reactions [2].
  • Our results support the original claimed specificity of PAO for the primary amino termini of polyamines, all of which are consistent with the general finding that the quinone-dependent copper amine oxidases specifically metabolize primary amines [2].
  • A method for determining bovine plasma amine oxidase (PAO; EC activity with benzylamine (Bz) as substrate is described [3].
  • Analysis of products formed from incubation of dopamine with PAO in tritiated water indicates a stereospecific, pro-R, incorporation of label at C-2 [4].

Biological context of PAOX

  • The gene order in Bos taurus is the same as in man, cen-ECHS1-PAOX-MTG1-SPRN-CYP2E1-tel, but PAOX has a different orientation in the two species [5].
  • Bovine plasma amine oxidase (PAO) has previously been shown to catalyze a nonstereospecific loss of tritium from [2(R)-3H]- and [2(S)-3H]dopamines, attributed to multiple, catalytically active binding sites for substrate [Summers, M. C., Markovic, R., & Klinman, J. P. (1979) Biochemistry 18, 1969-1979] [4].
  • Polyamine oxidase (PAO) is involved in polyamine metabolism and production of hydrogen peroxide in animal and plants, thus representing a key system in development and programmed cell death [6].

Anatomical context of PAOX

  • Macrophages contain polyamine oxidase, the reaction products of which are known to be similar to those of RPS polyamine oxidase but different from those of bovine polyamine oxidase [7].

Associations of PAOX with chemical compounds


  1. Trypanosoma brucei: polyamine oxidase mediated trypanolytic activity in the serum of naturally resistant cattle. Traore-Leroux, T., Fumoux, F., Chaize, J., Roelants, G.E. Exp. Parasitol. (1987) [Pubmed]
  2. Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini. Lee, Y., Sayre, L.M. J. Biol. Chem. (1998) [Pubmed]
  3. Michaelis-Menten analysis of bovine plasma amine oxidase by capillary electrophoresis using electrophoretically mediated microanalysis in a partially filled capillary. Van Dyck, S., Van Schepdael, A., Hoogmartens, J. Electrophoresis (2001) [Pubmed]
  4. Stereochemical probes of bovine plasma amine oxidase: evidence for mirror image processing and a syn abstraction of hydrogens from C-1 and C-2 of dopamine. Farnum, M.F., Klinman, J.P. Biochemistry (1986) [Pubmed]
  5. Cloning of the bovine prion-like Shadoo (SPRN) gene by comparative analysis of the predicted genomic locus. Uboldi, C., Paulis, M., Guidi, E., Bertoni, A., Meo, G.P., Perucatti, A., Iannuzzi, L., Raimondi, E., Brunner, R.M., Eggen, A., Ferretti, L. Mamm. Genome (2006) [Pubmed]
  6. Inhibition of pig liver and Zea mays L. polyamine oxidase: a comparative study. Federico, R., Leone, L., Botta, M., Binda, C., Angelini, R., Venturini, G., Ascenzi, P. J. Enzym. Inhib. (2001) [Pubmed]
  7. Polyamine oxidase in human retroplacental serum inhibits the growth of Plasmodium falciparum. Egan, J.E., Haynes, J.D., Brown, N.D., Eisemann, C.S. Am. J. Trop. Med. Hyg. (1986) [Pubmed]
  8. Polyamine oxidase-mediated intraerythrocytic killing of Plasmodium falciparum: evidence against the role of reactive oxygen metabolites. Rzepczyk, C.M., Saul, A.J., Ferrante, A. Infect. Immun. (1984) [Pubmed]
  9. Interaction of bovine serum amine oxidase with the polyamine oxidase inactivator MDL 72527. Agostinelli, E., Palmigiani, P., Vedova, L.D., Tempera, G., Belli, F., Seiler, N. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  10. Effects of glucocorticoids on polyamine metabolism in liver and spleen of guinea pig during sensitization. Bjelakovic, G., Pavlovic, D., Stojanovic, I., Jevtovic, T., Nikolic, J., Kocic, G. Amino Acids (2006) [Pubmed]
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