4.5 Article

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

Journal

FEBS LETTERS
Volume 589, Issue 20, Pages 3071-3078

Publisher

WILEY
DOI: 10.1016/j.febslet.2015.08.045

Keywords

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

Funding

  1. Ministry of Education, Culture, Sports, Science, and Technology of Japan (MEXT) [26.04081, 15K14705, 25-5682]
  2. JSPS postdoctoral fellowship
  3. Grants-in-Aid for Scientific Research [15K14705] Funding Source: KAKEN

Ask authors/readers for more resources

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, Se1PAO5 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 thermospennine at different carbon positions. We discuss the physiological significance of this difference. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available