The polyamine oxidase from lycophyte Selaginella lepidophylla (SelPAO5), unlike that of angiosperms, back-converts thermospermine to norspermidine

G. H.M. Sagor, Masataka Inoue, Dong Wook Kim, Seiji Kojima, Masaru Niitsu, Thomas Berberich, Tomonobu Kusano

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

In the phylogeny of plant polyamine oxidases (PAOs), clade III members from angiosperms, such as Arabidopsis thaliana PAO5 and Oryza sativa PAO1, prefer spermine and thermospermine as substrates and back-convert both of these substrates to spermidine in vitro. A clade III representative of lycophytes, SelPAO5 from Selaginella lepidophylla, also prefers spermine and thermospermine but instead back-converts these substrates to spermidine and norspermidine, respectively. This finding indicates that the clade III PAOs of lycophytes and angiosperms oxidize thermospermine at different carbon positions. We discuss the physiological significance of this difference.

Original languageEnglish
Article number37356
Pages (from-to)3071-3078
Number of pages8
JournalFEBS Letters
Volume589
Issue number20
DOIs
Publication statusPublished - 2015 Oct 7

Keywords

  • Norspermidine
  • Polyamine oxidase
  • Selaginella lepidophylla
  • Spermidine
  • Spermine
  • Thermospermine

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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