EC 1.5.3.17 - Non-specific polyamine oxidase

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IntEnz Enzyme Nomenclature
EC 1.5.3.17

Names

Accepted name:
non-specific polyamine oxidase
Other names:
polyamine oxidase [ambiguous]
Fms1
AtPAO3
Systematic name:
polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming)

Reactions

Cofactor

Comments:

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 [3]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [2]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [1]. The specific polyamine oxidases are classified as 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 1.5.3.16 (spermine oxidase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052904 , GO:0052903 , GO:0052902 , GO:0052901
UniProtKB/Swiss-Prot:

References

  1. Moschou, P. N., Sanmartin, M., Andriopoulou, A. H., Rojo, E., Sanchez-Serrano, J. J., Roubelakis-Angelakis, K. A.
    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: 1845-1857 (2008). [PMID: 18583528]
  2. Muller, S., Walter, R. D.
    Purification and characterization of polyamine oxidase from Ascaris suum.
    Biochem. J. 283: 75-80 (1992). [PMID: 1567380]
  3. Landry, J., Sternglanz, R.
    Yeast Fms1 is a FAD-utilizing polyamine oxidase.
    Biochem. Biophys. Res. Commun. 303: 771-776 (2003). [PMID: 12670477]

[EC 1.5.3.17 created 2009]