EC 1.5.3.16 - Spermine oxidase

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IntEnz Enzyme Nomenclature
EC 1.5.3.16

Names

Accepted name:
spermine oxidase
Other names:
PAOh1/SMO
PAOh1 [ambiguous]
AtPAO1
AtPAO4
SMO
mSMO
SMO(PAOh1)
SMO/PAOh1
SMO5
mSMOmu
Systematic name:
spermidine:oxygen oxidoreductase (spermidine-forming)

Reactions

Cofactor

Comments:

The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency [3]. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC 1.5.3.17 (non-specific polyamine oxidase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052895 , GO:0052894 , GO:0052901
UniProtKB/Swiss-Prot:

References

  1. Murray-Stewart, T., Wang, Y., Goodwin, A., Hacker, A., Meeker, A., Casero, R. A.
    Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology.
    FEBS J. 275: 2795-2806 (2008). [PMID: 18422650]
  2. Cervelli, M., Polticelli, F., Federico, R., Mariottini, P.
    Heterologous expression and characterization of mouse spermine oxidase.
    J. Biol. Chem. 278: 5271-5276 (2003). [PMID: 12458219]
  3. Tavladoraki, P., Rossi, M. N., Saccuti, G., Perez-Amador, M. A., Polticelli, F., Angelini, R., Federico, R.
    Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion.
    Plant Physiol. 141: 1519-1532 (2006). [PMID: 16778015]
  4. Wang, Y., Murray-Stewart, T., Devereux, W., Hacker, A., Frydman, B., Woster, P. M., Casero, R. A.
    Properties of purified recombinant human polyamine oxidase, PAOh1/SMO.
    Biochem. Biophys. Res. Commun. 304: 605-611 (2003). [PMID: 12727196]

[EC 1.5.3.16 created 2009]