Spermine oxidase

Spermine oxidase
Identifiers
EC no.1.5.3.16
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
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PDB structuresRCSB PDB PDBe PDBsum
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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] This enzyme catalyses the following chemical reaction

2D representation of the chemical structure of spermine.
spermine
+ H2O
 
 
O2
H2O2
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
O2
H2O2
 
2D representation of the chemical structure of spermidine.
spermidine
+
 
2D representation of the chemical structure of Q22984448.
3-aminopropanal

The enzyme from Arabidopsis thaliana oxidizes norspermine to norspermidine.[4]

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. ↑ 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. Bibcode:2003BBRC..304..605W. doi:10.1016/S0006-291X(03)00636-3. PMID 12727196.
  4. ↑ 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.
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