Biology:Spermine oxidase
From HandWiki
| 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 [math]\displaystyle{ \rightleftharpoons }[/math] spermidine + 3-aminopropanal + H2O2
The enzyme from Arabidopsis thaliana oxidizes norspermine to norspermidine.
References
- ↑ "Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology". The FEBS Journal 275 (11): 2795–806. Jun 2008. doi:10.1111/j.1742-4658.2008.06419.x. PMID 18422650.
- ↑ "Heterologous expression and characterization of mouse spermine oxidase". The Journal of Biological Chemistry 278 (7): 5271–6. Feb 2003. doi:10.1074/jbc.M207888200. PMID 12458219.
- ↑ "Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion". Plant Physiology 141 (4): 1519–32. Aug 2006. doi:10.1104/pp.106.080911. PMID 16778015.
- ↑ "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO". Biochemical and Biophysical Research Communications 304 (4): 605–11. May 2003. doi:10.1016/S0006-291X(03)00636-3. PMID 12727196.
External links
- Spermine+oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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