Spermine oxidase

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

\rightleftharpoons

spermidine + 3-aminopropanal + H₂O₂

The enzyme from Arabidopsis thaliana oxidizes norspermine to norspermidine.

References

↑ 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. PMID 18422650.
↑ 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.
↑ 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.
↑ 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.

Spermine oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: CH-NH (EC 1.5)

1.5.1: NAD or NADP acceptor	Dihydrofolate reductase Saccharopine dehydrogenase Methylenetetrahydrofolate reductase

1.5.3: oxygen acceptor	Dihydrobenzophenanthridine oxidase Sarcosine oxidase Proline oxidase

1.5.5: quinone acceptor	Electron-transferring-flavoprotein dehydrogenase

1.5.99	Sarcosine dehydrogenase Cytokinin dehydrogenase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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