Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store

MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:,

Enzymes and Genes:

Arabidopsis thaliana col: spermine oxidaseInferred from experiment: PAO1
spermine oxidaseInferred from experiment: PAO4
non-specific polyamine oxidaseInferred from experiment: PAO3
Homo sapiens: polyamine oxidase 1 (spermidine-forming)Inferred from experiment: SMOX
Saccharomyces cerevisiae: non-specific polyamine oxidaseInferred from experiment: FMS1

In Pathway: spermine and spermidine degradation I, spermine and spermidine degradation III, β-alanine biosynthesis IV

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name for spermine oxidase

Enzyme Commission Synonyms for PAOh1/SMO, PAOh1 (ambiguous), AtPAO1, AtPAO4, SMO, mSMO, SMO(PAOh1), SMO/PAOh1, SMO5, mSMOmu

Enzyme Commission Primary Name for non-specific polyamine oxidase

Enzyme Commission Synonyms for polyamine oxidase (ambiguous), Fms1, AtPAO3

Standard Gibbs Free Energy (ΔrG in kcal/mol): -21.580688Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for
The enzyme from Arabidopsis thaliana ( PAO1) oxidizes norspermine to norspermidine with high efficiency. 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 (N1-acetylpolyamine oxidase), EC (polyamine oxidase (propane-1,3-diamine-forming)), EC (N8-acetylspermidine oxidase (propane-1,3-diamine-forming) and EC (non-specific polyamine oxidase).

Enzyme Commission Summary for
A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [Landry03]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [Muller92a]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [Moschou08]. The specific polyamine oxidases are classified as EC (N1-acetylpolyamine oxidase), EC (polyamine oxidase (propane-1,3-diamine-forming)), EC (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC (spermine oxidase).

Citations: [Wang03a, Tavladoraki06, Cervelli03, MurrayStewart08]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R09076, Rhea:25804

Relationship Links: BRENDA:EC:, BRENDA:EC:, ENZYME:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, IUBMB-ExplorEnz:EC:

Revised 05-Aug-2009 by Caspi R, SRI International


Cervelli03: Cervelli M, Polticelli F, Federico R, Mariottini P (2003). "Heterologous expression and characterization of mouse spermine oxidase." J Biol Chem 278(7);5271-6. PMID: 12458219

Landry03: Landry J, Sternglanz R (2003). "Yeast Fms1 is a FAD-utilizing polyamine oxidase." Biochem Biophys Res Commun 303(3);771-6. PMID: 12670477

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Moschou08: Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA (2008). "Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis." Plant Physiol 147(4);1845-57. PMID: 18583528

Muller92a: Muller S, Walter RD (1992). "Purification and characterization of polyamine oxidase from Ascaris suum." Biochem J 283 ( Pt 1);75-80. PMID: 1567380

MurrayStewart08: Murray-Stewart T, Wang Y, Goodwin A, Hacker A, Meeker A, Casero RA (2008). "Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology." FEBS J 275(11);2795-806. PMID: 18422650

Tavladoraki06: Tavladoraki P, Rossi MN, Saccuti G, Perez-Amador MA, Polticelli F, Angelini R, Federico R (2006). "Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion." Plant Physiol 141(4);1519-32. PMID: 16778015

Wang03a: Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA (2003). "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO." Biochem Biophys Res Commun 304(4);605-11. PMID: 12727196

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc14.