ExplorEnz: EC 1.5.3.16

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1.5.3.16

Accepted name:

spermine oxidase

Reaction:

spermine + O₂ + H₂O = spermidine + 3-aminopropanal + H₂O₂

Other name(s):

PAOh1/SMO; PAOh1 (ambiguous); AtPAO1; AtPAO4; SMO; mSMO; SMO(PAOh1); SMO/PAOh1; SMO5; mSMOmu

Systematic name:

spermidine:oxygen oxidoreductase (spermidine-forming)

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:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

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

[EC 1.5.3.16 created 2009]