Oxidoreductases;
Acting on the CH-NH group of donors;
With oxygen as acceptor

N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming)

(1) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2 [RN:R09074];
(2) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2 [RN:R03899]

R03899 R09074

N1-acetylspermidine [CPD:C00612];
O2 [CPD:C00007];
H2O [CPD:C00001];
N1-acetylspermine [CPD:C02567]

The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 [1]. No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 [2]. A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from 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)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).

EC 1.5.3.13 created 2009

1  [PMID:12477380]

Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW

Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion.

Biochem. J. 370 (2003) 19-28.

[hsa:196743]

2  [PMID:15611107]

Jarvinen A, Grigorenko N, Khomutov AR, Hyvonen MT, Uimari A, Vepsalainen J, Sinervirta R, Keinanen TA, Vujcic S, Alhonen L, Porter CW, Janne J

Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural polyamines.

J. Biol. Chem. 280 (2005) 6595-601.

3  [PMID:15791459]

Wang Y, Hacker A, Murray-Stewart T, Frydman B, Valasinas A, Fraser AV, Woster PM, Casero RA Jr

Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity.

Cancer. Chemother. Pharmacol. 56 (2005) 83-90.

4  [PMID:12660232]

Wu T, Yankovskaya V, McIntire WS

Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase.

J. Biol. Chem. 278 (2003) 20514-25.

[mmu:212503]