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J. Biol. Chem., Vol. 278, Issue 7, 5271-5276, February 14, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/7/5271    most recent M207888200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Cervelli, M. Articles by Mariottini, P. Search for Related Content PubMed PubMed Citation Articles by Cervelli, M. Articles by Mariottini, P. Social Bookmarking                      What's this?

Heterologous Expression and Characterization of Mouse Spermine Oxidase^*

Manuela Cervelli, Fabio Polticelli, Rodolfo Federico, and Paolo Mariottini

From the Dipartimento di Biologia, Università "Roma Tre," I-00146 Roma, Italy

Polyamine oxidases are key enzymes responsible of the polyamine interconversion metabolism in animal cells. Recently, a novel enzyme belonging to this class of enzymes has been characterized for its capability to oxidize preferentially spermine and designated as spermine oxidase. This is a flavin adenine dinucleotide-containing enzyme, and it has been expressed both in vitro and in vivo systems. The primary structure of mouse spermine oxidase (mSMO) was deduced from a cDNA clone (Image Clone 264769) recovered by a data base search utilizing the human counterpart of polyamine oxidases, PAOh1. The open reading frame predicts a 555-amino acid protein with a calculated M_r of 61,852.30, which shows a 95.1% identity with PAOh1. To understand the biochemical properties of mSMO and its structure/function relationship, the mSMO cDNA has been subcloned and expressed in secreted and secreted-tagged forms into Escherichia coli BL21 DE3 cells. The recombinant enzyme shows an optimal pH value of 8.0 and is able to oxidize rapidly spermine to spermidine and 3-aminopropanal and fails to act upon spermidine and N¹-acetylpolyamines. The purified recombinant-tagged form enzyme (M_r ~68,000) has K_m and k_cat values of 90 µM and 4.5 s¹, respectively, using spermine as substrate at pH 8.0. Molecular modeling of mSMO protein based on maize polyamine oxidase three-dimensional structure suggests that the general features of maize polyamine oxidase active site are conserved in mSMO.

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