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MetaCyc Reaction: 1.5.3.16/1.5.3.17

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

EC Number: 1.5.3.16 , 1.5.3.17

Enzymes and Genes:
non-specific polyamine oxidase Inferred from experiment : FMS1 ( Saccharomyces cerevisiae )
non-specific polyamine oxidase Inferred from experiment : PAO3 ( Arabidopsis thaliana col )
spermine oxidase Inferred from experiment : PAO4 ( Arabidopsis thaliana col )
spermine oxidase Inferred from experiment : PAO1 ( Arabidopsis thaliana col )
polyamine oxidase 1 (spermidine-forming) Inferred from experiment : SMOX ( Homo sapiens )

In Pathway: spermine and spermidine degradation I , spermine and spermidine degradation III , β-alanine biosynthesis IV

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name for 1.5.3.16: spermine oxidase

Enzyme Commission Synonyms for 1.5.3.16: PAOh1/SMO, PAOh1 (ambiguous), AtPAO1, AtPAO4, SMO, mSMO, SMO(PAOh1), SMO/PAOh1, SMO5, mSMOmu

Enzyme Commission Primary Name for 1.5.3.17: non-specific polyamine oxidase

Enzyme Commission Synonyms for 1.5.3.17: polyamine oxidase (ambiguous), Fms1, AtPAO3

Standard Gibbs Free Energy (ΔrG in kcal/mol): -21.580688 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for 1.5.3.16:
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).

Enzyme Commission Summary for 1.5.3.17:
A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [Landry03]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [Muller92a]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [Moschou08]. The specific polyamine oxidases are classified as 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 1.5.3.16 (spermine oxidase).

Citations: [Wang03c, Tavladoraki06, Cervelli03, MurrayStewart08]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R09076 , Rhea:25804

Relationship Links: BRENDA:EC:1.5.3.16 , BRENDA:EC:1.5.3.17 , ENZYME:EC:1.5.3.16 , ENZYME:EC:1.5.3.17 , IUBMB-ExplorEnz:EC:1.5.3.16 , IUBMB-ExplorEnz:EC:1.5.3.17

Credits:
Revised 05-Aug-2009 by Caspi R , SRI International


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."

Moschou08: Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA (2008). "Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis." Plant Physiol 147(4);1845-57. PMID: 18583528

Muller92a: Muller S, Walter RD (1992). "Purification and characterization of polyamine oxidase from Ascaris suum." Biochem J 283 ( Pt 1);75-80. PMID: 1567380

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, biocyc12.