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 oxidase
Identifiers
EC no.1.5.3.16
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
spermine + O2 + H2O spermidine + 3-aminopropanal + H2O2

The enzyme from Arabidopsis thaliana oxidizes norspermine to norspermidine.

References

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  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. ^ 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. ^ 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. ^ 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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