Spermine_oxidase

Spermine oxidase

Spermine oxidase

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Spermine oxidase (EC 1.5.3.16, PAOh1/SMO, AtPAO1, AtPAO4, SMO) is an enzyme with systematic name spermidine:oxygen oxidoreductase (spermidine-forming).[1][2][3][4] This enzyme catalyses the following chemical reaction

spermine + O2 + H2O spermidine + 3-aminopropanal + H2O2
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The enzyme from Arabidopsis thaliana oxidizes norspermine to norspermidine.

References

  1. [1]
    Murray-Stewart T, Wang Y, Goodwin A, Hacker A, Meeker A, Casero RA (Jun 2008). "Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology". The FEBS Journal. 275 (11): 2795–806. doi:10.1111/j.1742-4658.2008.06419.x. PMC 3631774. PMID 18422650.
  2. [2]
    Cervelli M, Polticelli F, Federico R, Mariottini P (Feb 2003). "Heterologous expression and characterization of mouse spermine oxidase". The Journal of Biological Chemistry. 278 (7): 5271–6. doi:10.1074/jbc.M207888200. PMID 12458219.
  3. [3]
    Tavladoraki P, Rossi MN, Saccuti G, Perez-Amador MA, Polticelli F, Angelini R, Federico R (Aug 2006). "Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion". Plant Physiology. 141 (4): 1519–32. doi:10.1104/pp.106.080911. PMC 1533960. PMID 16778015.
  4. [4]
    Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA (May 2003). "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO". Biochemical and Biophysical Research Communications. 304 (4): 605–11. doi:10.1016/S0006-291X(03)00636-3. PMID 12727196.
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