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MetaCyc Reaction: 1.5.3.13/1.5.3.17

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

EC Number: 1.5.3.13 , 1.5.3.17

Enzymes and Genes:
N1-acetylpolyamine oxidase (3-acetamamidopropanal -forming) Inferred from experiment : Paox ( Mus musculus )
non-specific polyamine oxidase Inferred from experiment : FMS1 ( Saccharomyces cerevisiae )

In Pathway: spermine and spermidine degradation I

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 1.5.3.13: N1-acetylpolyamine oxidase

Enzyme Commission Synonyms for 1.5.3.13: hPAO-1, PAO (ambiguous), mPAO, hPAO, polyamine oxidase (ambiguous)

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): -23.453003 Inferred by computational analysis [Latendresse13]

Summary:
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 [Muller92]. 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).

Enzyme Commission Summary for 1.5.3.13:
A flavoprotein (FAD). This enzyme, encoded by the Paox gene, is found in mammalian peroxisomes and oxidizes N(1)-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion.

The enzyme also catalyzes the reaction: N1,N12-diacetylspermine + oxygen + H2O → N1-acetylspermidine + 3-acetamidopropanal + hydrogen peroxide [Vujcic03].

The enzyme has no or very weak activity with spermine or spermidine in absence of aldehydes. However, in presence of aldehydes the enzyme also catalyzes the reactions:

spermine + oxygen + H2O → spermidine + 3-aminopropanal + hydrogen peroxide and (with weak efficiency) spermidine + oxygen + H2O → putrescine + 3-aminopropanal + hydrogen peroxide [Jarvinen05].

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 [Muller92]. 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: [Wang05, Wu03, Wanders06]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R09074 , Rhea:25812

Relationship Links: BRENDA:EC:1.5.3.13 , BRENDA:EC:1.5.3.17 , ENZYME:EC:1.5.3.13 , ENZYME:EC:1.5.3.17 , IUBMB-ExplorEnz:EC:1.5.3.13 , IUBMB-ExplorEnz:EC:1.5.3.17

Credits:
Created 24-Jan-2011 by Caspi R , SRI International


References

Jarvinen05: Jarvinen A, Grigorenko N, Khomutov AR, Hyvonen MT, Uimari A, Vepsalainen J, Sinervirta R, Keinanen TA, Vujcic S, Alhonen L, Porter CW, Janne J (2005). "Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural polyamines." J Biol Chem 280(8);6595-601. PMID: 15611107

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

Muller92: Muller S, Walter RD (1992). "Purification and characterization of polyamine oxidase from Ascaris suum." Biochem J 283 ( Pt 1);75-80. PMID: 1567380

Vujcic03: Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW (2003). "Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion." Biochem J 370(Pt 1);19-28. PMID: 12477380

Wanders06: Wanders RJ, Waterham HR (2006). "Biochemistry of mammalian peroxisomes revisited." Annu Rev Biochem 75;295-332. PMID: 16756494

Wang05: Wang Y, Hacker A, Murray-Stewart T, Frydman B, Valasinas A, Fraser AV, Woster PM, Casero RA (2005). "Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity." Cancer Chemother Pharmacol 56(1);83-90. PMID: 15791459

Wu03: Wu T, Yankovskaya V, McIntire WS (2003). "Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase." J Biol Chem 278(23);20514-25. PMID: 12660232


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 Mon Dec 22, 2014, biocyc13.