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MetaCyc Reaction: 1.5.3.16

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.5.3.16

Enzymes and Genes:

Arabidopsis thaliana col : spermine oxidase Inferred from experiment : PAO1

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name: spermine oxidase

Enzyme Commission Synonyms: PAOh1/SMO, PAOh1 (ambiguous), AtPAO1, AtPAO4, SMO, mSMO, SMO(PAOh1), SMO/PAOh1, SMO5, mSMOmu

Taxonomic Range: Viridiplantae , Metazoa

Standard Gibbs Free Energy (ΔrG in kcal/mol): -21.580627 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme from Arabidopsis thaliana (PAO1) oxidizes norspermine to norspermidine with high efficiency. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming) and EC 1.5.3.17 (non-specific polyamine oxidase).

Citations: [Tavladoraki06, Wang03c, Cervelli03, MurrayStewart08, Landry03]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Unification Links: Rhea:25816

Relationship Links: BRENDA:EC:1.5.3.16 , ENZYME:EC:1.5.3.16 , IUBMB-ExplorEnz:EC:1.5.3.16


References

Cervelli03: Cervelli M, Polticelli F, Federico R, Mariottini P (2003). "Heterologous expression and characterization of mouse spermine oxidase." J Biol Chem 278(7);5271-6. PMID: 12458219

Landry03: Landry J, Sternglanz R (2003). "Yeast Fms1 is a FAD-utilizing polyamine oxidase." Biochem Biophys Res Commun 303(3);771-6. PMID: 12670477

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

MurrayStewart08: Murray-Stewart T, Wang Y, Goodwin A, Hacker A, Meeker A, Casero RA (2008). "Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology." FEBS J 275(11);2795-806. PMID: 18422650

Tavladoraki06: Tavladoraki P, Rossi MN, Saccuti G, Perez-Amador MA, Polticelli F, Angelini R, Federico R (2006). "Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion." Plant Physiol 141(4);1519-32. PMID: 16778015

Wang03c: Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA (2003). "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO." Biochem Biophys Res Commun 304(4);605-11. PMID: 12727196


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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