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Published on June 15, 2006; 10.1104/pp.106.080911

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Received March 27, 2006
Returned for revision May 9, 2006
Accepted May 15, 2006

Heterologous Expression and Biochemical Characterization of a Polyamine Oxidase from Arabidopsis thaliana involved in Polyamine Back-Conversion

Paraskevi Tavladoraki *, Marianna Nicoletta Rossi , Giuseppe Saccuti , Miguel Angel Perez-Amador , Fabio Polticelli , Riccardo Angelini , and Rodolfo Federico

Department of Biology, University ‘Roma Tre’, 00146 Rome, Italy
Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia, Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain

* Corresponding author; email: tavlador{at}uniroma3.it.

Polyamine oxidase (PAO) is a FAD-dependent enzyme involved in polyamine catabolism. Animal PAO oxidize spermine or spermidine (and/or their acetyl derivatives) to produce H2O2, an aminoaldehyde and spermidine or putrescine, respectively, thus being involved in a polyamine back-conversion pathway. On the contrary, the plant PAO which have been characterized to date oxidize spermine and spermidine to produce 1,3-diaminopropane, H2O2 and an aminoaldehyde and are therefore involved in the terminal catabolism of polyamines. A database search within the Arabidopsis thaliana genome sequence showed the presence of a gene (AtPAO1) encoding for a putative PAO with 45% amino acid sequence identity with maize PAO. The AtPAO1 cDNA was isolated and cloned in a vector for heterologous expression in Escherichia coli. The recombinant protein was purified by affinity chromatography on guazatine-Sepharose 4B and was shown to be a flavoprotein able to oxidize spermine, norspermine and N 1-acetylspermine with a pH optimum at 8.0. Analysis of the reaction products showed that AtPAO1 produces spermidine from spermine and norspermidine from norspermine, demonstrating a substrate oxidation mode similar to that of animal PAO. To our knowledge, AtPAO1 is the first plant PAO reported to be involved in a polyamine back-conversion pathway.




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T. Kamada-Nobusada, M. Hayashi, M. Fukazawa, H. Sakakibara, and M. Nishimura
A Putative Peroxisomal Polyamine Oxidase, AtPAO4, is Involved in Polyamine Catabolism in Arabidopsis thaliana
Plant Cell Physiol., September 1, 2008; 49(9): 1272 - 1282.
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