PMID:9598979 (1.5.3.14)

Tavladoraki P, Schinina ME, Cecconi F, Di Agostino S, Manera F, Rea G, Mariottini P, Federico R, Angelini R

Maize polyamine oxidase: primary structure from protein and cDNA sequencing.

FEBS Lett 426:62-6 (1998)
DOI:10.1016/S0014-5793(98)00311-1

[zma:541983]

PMID:16778015 (1.5.3.16)

Tavladoraki P, Rossi MN, Saccuti G, Perez-Amador MA, Polticelli F, Angelini R, Federico R

Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion.

Plant Physiol 141:1519-32 (2006)
DOI:10.1104/pp.106.080911

[ath:AT5G13700]

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

spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)

spermidine + O2 + H2O = propane-1,3-diamine + 4-aminobutanal + H2O2 [RN:R01914]

R01914
Reaction

spermidine [CPD:C00315];
O2 [CPD:C00007];
H2O [CPD:C00001]

As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines [1]. This enzyme less efficiently catalyses the oxidation of N1-acetylspermine and spermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), 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 1.5.3.14 created 2009

1  [PMID:9598979]

Tavladoraki P, Schinina ME, Cecconi F, Di Agostino S, Manera F, Rea G, Mariottini P, Federico R, Angelini R

Maize polyamine oxidase: primary structure from protein and cDNA sequencing.

FEBS Lett 426:62-6 (1998)
DOI:10.1016/S0014-5793(98)00311-1

[zma:541983]

2

Federico, R., Ercolini, L., Laurenzi, M., Angelini, R.

Oxidation of acetylpolyamines by maize polyamine oxidase.

Phytochemistry 43:339-341 (1996)