PMID- 29063977
OWN - NLM
STAT- MEDLINE
DCOM- 20180813
LR  - 20231213
IS  - 1618-0860 (Electronic)
IS  - 0918-9440 (Linking)
VI  - 131
IP  - 2
DP  - 2018 Mar
TI  - Highly-expressed polyamine oxidases catalyze polyamine back conversion in 
      Brachypodium distachyon.
PG  - 341-348
LID - 10.1007/s10265-017-0989-2 [doi]
AB  - To understand the polyamine (PA) catabolic pathways in Brachypodium distachyon, 
      we focused on the flavin-containing polyamine oxidase enzymes (PAO), and 
      characterized them at the molecular and biochemical levels. Five PAO isoforms 
      were identified from database searches, and we named them BdPAO1 to BdPAO5. By 
      gene expression analysis using above-ground tissues such as leaf, stem and 
      inflorescence, it was revealed that BdPAO2 is the most abundant PAO gene in 
      normal growth conditions, followed by BdPAO3 and BdPAO4. BdPAO1 and BdPAO5 were 
      expressed at very low levels. All Arabidopsis thaliana and rice orthologs 
      belonging to the same clade as BdPAO2, BdPAO3 and BdPAO4 have conserved 
      peroxisome-targeting signal sequences at their C-termini. Amino acid sequences of 
      BdPAO2 and BdPAO4 also showed such a sequence, but BdPAO3 did not. We selected 
      the gene with the highest expression level (BdPAO2) and the peroxisome-targeting 
      signal lacking PAO (BdPAO3) for biochemical analysis of substrate specificity and 
      catabolic pathways. BdPAO2 catalyzed conversion of spermine (Spm) or 
      thermospermine to spermidine (Spd), and Spd to putrescine, but its most-favored 
      substrate was Spd. In contrast, BdPAO3 favored Spm as substrate and catalyzed 
      conversion of tetraamines to Spd. These results indicated that the major PAOs in 
      B. distachyon have back-conversion activity.
FAU - Takahashi, Yoshihiro
AU  - Takahashi Y
AD  - Department of Applied Chemistry and Biochemistry, Faculty of Engineering, Kyushu 
      Sangyo University, 2-3-1 Matsukadai Higashi-ku, Fukuoka, 813-8503, Japan. 
      ytaka@ip.kyusan-u.ac.jp.
FAU - Ono, Kaede
AU  - Ono K
AD  - Department of Applied Chemistry and Biochemistry, Faculty of Engineering, Kyushu 
      Sangyo University, 2-3-1 Matsukadai Higashi-ku, Fukuoka, 813-8503, Japan.
FAU - Akamine, Yuuta
AU  - Akamine Y
AD  - Department of Applied Chemistry and Biochemistry, Faculty of Engineering, Kyushu 
      Sangyo University, 2-3-1 Matsukadai Higashi-ku, Fukuoka, 813-8503, Japan.
FAU - Asano, Takuya
AU  - Asano T
AD  - Department of Applied Chemistry and Biochemistry, Faculty of Engineering, Kyushu 
      Sangyo University, 2-3-1 Matsukadai Higashi-ku, Fukuoka, 813-8503, Japan.
FAU - Ezaki, Masatoshi
AU  - Ezaki M
AD  - Department of Applied Chemistry and Biochemistry, Faculty of Engineering, Kyushu 
      Sangyo University, 2-3-1 Matsukadai Higashi-ku, Fukuoka, 813-8503, Japan.
FAU - Mouri, Itsupei
AU  - Mouri I
AD  - Department of Applied Chemistry and Biochemistry, Faculty of Engineering, Kyushu 
      Sangyo University, 2-3-1 Matsukadai Higashi-ku, Fukuoka, 813-8503, Japan.
LA  - eng
PT  - Journal Article
DEP - 20171024
PL  - Japan
TA  - J Plant Res
JT  - Journal of plant research
JID - 9887853
RN  - 0 (Plant Proteins)
RN  - 0 (Polyamines)
RN  - EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors)
SB  - IM
MH  - Amino Acid Sequence
MH  - Brachypodium/*genetics
MH  - *Gene Expression
MH  - Metabolic Networks and Pathways/genetics
MH  - Oxidoreductases Acting on CH-NH Group Donors/chemistry/*genetics/metabolism
MH  - Phylogeny
MH  - Plant Proteins/chemistry/*genetics/metabolism
MH  - Polyamines/*metabolism
MH  - Sequence Alignment
MH  - Polyamine Oxidase
OTO - NOTNLM
OT  - Back-conversion
OT  - Brachypodium distachyon
OT  - Peroxisome-targeting signal
OT  - Polyamine oxidase
OT  - Spermidine
OT  - Spermine
EDAT- 2017/10/25 06:00
MHDA- 2018/08/14 06:00
CRDT- 2017/10/25 06:00
PHST- 2017/07/05 00:00 [received]
PHST- 2017/10/04 00:00 [accepted]
PHST- 2017/10/25 06:00 [pubmed]
PHST- 2018/08/14 06:00 [medline]
PHST- 2017/10/25 06:00 [entrez]
AID - 10.1007/s10265-017-0989-2 [pii]
AID - 10.1007/s10265-017-0989-2 [doi]
PST - ppublish
SO  - J Plant Res. 2018 Mar;131(2):341-348. doi: 10.1007/s10265-017-0989-2. Epub 2017 
      Oct 24.