Spermine oxidase

Spermine oxidase
Identifiers
EC number 1.5.3.16
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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 + O2 + H2O spermidine + 3-aminopropanal + H2O2

The enzyme from Arabidopsis thaliana oxidizes norspermine to norspermidine.

References

  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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