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Information on EC 1.5.3.17 - non-specific polyamine oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LYT1
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1.5.3.17 non-specific polyamine oxidaseIUBMB Comments
A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine . The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine . The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines .
The specific polyamine oxidases are classified as EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC 1.5.3.16 (spermine oxidase).
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Word Map
- 1.5.3.17
- spermidine
-
back-conversion
- putrescine
- peroxisomal
- sativa
- seedling
-
tetraamines
-
abscisic
- anther
- pollen
- medicine
- analysis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
atpao5, atpao2, atpao3, ospao1, atpao4, polyamine oxidase 1, selpao5, bjpao2, bjpao1, slr5093, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming)
A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [3]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [2]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [1].
The specific polyamine oxidases are classified as EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC 1.5.3.16 (spermine oxidase).
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
?
the enzyme AtPAO5 has a better activity as a dehydrogenase rather than as an oxidase. With the best electron acceptor (ferricenium), the best in vitro substrate for recombinant AtPAO5 is N1-acetylspermine
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
about 10% of the activity with spermidine
-
-
?
norspermine + O2 + H2O
? + H2O2
about 40% of the activity with spermidine
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
best substrate
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
best substrate
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
about 60% of the activity with spermidine
-
-
?
thermospermine + O2 + H2O
? + H2O2
about 30% of the activity with spermidine
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
at pH 6.5, substrate preference is in the following decreasing order: thermospermine, N1-acetylspermine, norspermine, spermine, spermidine. Spermidine is catabolized at a very low rate. At pH 7.5, substrate preference is in the following decreasing order: spermine, norspermine, N1-acetylspermine, thermospermine, spermidine. Spermidine is catalyzed at a very low rate
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
about 10% of the activity with spermidine
-
-
?
norspermine + O2 + H2O
?
at pH 6.5, substrate preference is in the following decreasing order: thermospermine, N1-acetylspermine, norspermine, spermine, spermidine. Spermidine is catabolized at a very low rate. At pH 7.5, substrate preference is in the following decreasing order: spermine, norspermine, N1-acetylspermine, thermospermine, spermidine. Spermidine is catalyzed at a very low rate
-
-
?
norspermine + O2 + H2O
?
the enzyme AtPAO5 has a better activity as a dehydrogenase rather than as an oxidase. With the best electron acceptor (ferricenium), the best in vitro substrate for recombinant AtPAO5 is N1-acetylspermine
-
-
?
norspermine + O2 + H2O
? + H2O2
about 45% of the activity with spermidine
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
best substrate
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
at pH 6.5, substrate preference is in the following decreasing order: thermospermine, N1-acetylspermine, norspermine, spermine, spermidine. Spermidine is catabolized at a very low rate. At pH 7.5, substrate preference is in the following decreasing order: spermine, norspermine, N1-acetylspermine, thermospermine, spermidine. Spermidine is catalyzed at a very low rate
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
at pH 6.5, substrate preference is in the following decreasing order: thermospermine, N1-acetylspermine, norspermine, spermine, spermidine. Spermidine is catabolized at a very low rate. At pH 7.5, substrate preference is in the following decreasing order: spermine, norspermine, N1-acetylspermine, thermospermine, spermidine. Spermidine is catalyzed at a very low rate
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme AtPAO5 catabolizes the thermospermine and spermine tetraamines to spermidine and marginally to putrescine
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme AtPAO5 has a better activity as a dehydrogenase rather than as an oxidase. With the best electron acceptor (ferricenium), the best in vitro substrate for recombinant AtPAO5 is N1-acetylspermine
-
-
?
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
about 60% of the activity with spermidine
-
-
?
thermospermine + O2 + H2O
?
the enzyme AtPAO5 has a better activity as a dehydrogenase rather than as an oxidase. With the best electron acceptor (ferricenium), the best in vitro substrate for recombinant AtPAO5 is N1-acetylspermine
-
-
?
thermospermine + O2 + H2O
? + H2O2
about 30% of the activity with spermidine
-
-
?
thermospermine + O2 + H2O
spermidine + ?
at pH 6.5, substrate preference is in the following decreasing order: thermospermine, N1-acetylspermine, norspermine, spermine, spermidine. Spermidine is catabolized at a very low rate. At pH 7.5, substrate preference is in the following decreasing order: spermine, norspermine, N1-acetylspermine, thermospermine, spermidine. Spermidine is catalyzed at a very low rate. At pH 6.5, all thermospermine substrate is converted to spermidine within 30 min. A very low putrescine level is detected at 30 min. The conversion of thermospermine to spermidine is reduced at pH 6.0, and only tiny amounts of putrescine are observed
-
-
?
thermospermine + O2 + H2O
spermidine + ?
the enzyme AtPAO5 catabolizes the thermospermine and spermine tetraamines to spermidine and marginally to putrescine
-
-
?
additional information
?
-
no activity with agmatine, cadaverine, and putrescine
-
-
?
additional information
?
-
AtPAO3 catalyzes the sequential conversion/oxidation of spermine to spermidine, and of spermidine to putrescine, thus exhibiting functional homology to the mammalian PAOs, but AtPAO3 does not catalyze the conversion of putrescine back to spermine
-
-
?
additional information
?
-
substrate specificity of AtPAO3, the best substrate is Spd, whereas the N1-acetyl-derivatives of spermine and spermidine are oxidized less efficiently, no activity with diamines agmatine, cadaverine, and putrescine. AtPAO3 does not catalyze the conversion of putrescine back to spermine
-
-
?
additional information
?
-
comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
-
comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
AtPAO3 is twofold more active with spermidine than with spermine
-
-
?
additional information
?
-
AtPAO3 is twofold more active with spermidine than with spermine
-
-
?
additional information
?
-
AtPAO3 is twofold more active with spermidine than with spermine
-
-
?
additional information
?
-
-
AtPAO3 is twofold more active with spermidine than with spermine
-
-
?
additional information
?
-
comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
-
comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
AtPAO2 is equally active with spermine and spermidine
-
-
?
additional information
?
-
AtPAO2 is equally active with spermine and spermidine
-
-
?
additional information
?
-
AtPAO2 is equally active with spermine and spermidine
-
-
?
additional information
?
-
-
AtPAO2 is equally active with spermine and spermidine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
additional information
?
-
AtPAO3 catalyzes the sequential conversion/oxidation of spermine to spermidine, and of spermidine to putrescine, thus exhibiting functional homology to the mammalian PAOs, but AtPAO3 does not catalyze the conversion of putrescine back to spermine
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
AtPAO4 is rapidly inactivated under high ionic strength conditions
additional information
AtPAO4 is rapidly inactivated under high ionic strength conditions
additional information
AtPAO4 is rapidly inactivated under high ionic strength conditions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
N1-acetylspermine
pH 7.5, temperature not specified in the publication
0.045
norspermine
pH 7.5, temperature not specified in the publication
0.274
spermidine
pH 7.5, temperature not specified in the publication
0.58
spermine
pH 7.5, temperature not specified in the publication
0.05
thermospermine
pH 7.5, temperature not specified in the publication
0.233
N1-acetylspermine
pH 7.5, temperature not specified in the publication
0.409
spermidine
pH 7.5, temperature not specified in the publication
0.27
spermine
pH 7.5, temperature not specified in the publication
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
N1-acetylspermine
pH 7.5, temperature not specified in the publication
1.1
norspermine
pH 7.5, temperature not specified in the publication
3.4
spermidine
pH 7.5, temperature not specified in the publication
1.7
spermine
pH 7.5, temperature not specified in the publication
0.5
thermospermine
pH 7.5, temperature not specified in the publication
0.8
N1-acetylspermine
pH 7.5, temperature not specified in the publication
2.9
norspermine
pH 7.5, temperature not specified in the publication
4.6
spermidine
pH 7.5, temperature not specified in the publication
4.2
spermine
pH 7.5, temperature not specified in the publication
0.4
thermospermine
pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
N1-acetylspermine
pH 7.5, temperature not specified in the publication
24.4
norspermine
pH 7.5, temperature not specified in the publication
12.4
spermidine
pH 7.5, temperature not specified in the publication
2.9
spermine
pH 7.5, temperature not specified in the publication
10
thermospermine
pH 7.5, temperature not specified in the publication
3.4
N1-acetylspermine
pH 7.5, temperature not specified in the publication
11.2
spermidine
pH 7.5, temperature not specified in the publication
15.6
spermine
pH 7.5, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
pH 7: about 95% of maximal activity, pH 8.5: about 55% of maximal activity
6 - 10
pH 6.0: about 65% of maximal activity, pH 10.0: about 35% of maximal activity, substrate: thermospermine
7 - 9
pH 7.0: about 60% of maximal activity, pH 9.0: about 45% of maximal activity, substrate: spermine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
30°C: about 85% of maximal activity, 40°C: about 60% of maximal activity
25 - 50
25 - 50
25°C: about 45% of maximal activity, 50°C: about 90% of maximal activity, substrate: thermospermine
25 - 50
25°C: about 55% of maximal activity, 50°C: about 45% of maximal activity, substrate: spermine
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.81
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression at higher extent in the later growth stage within restricted parts of the organs, such as shoot meristem, leaf petiole and also in anther
already in very young, completely closed flower buds
expression at higher extent in the later growth stage within restricted parts of the organs, such as shoot meristem, leaf petiole and also in anther
in mature pollen grains during pollination and pollen tube growth
expression at higher extent in the later growth stage within restricted parts of the organs, such as shoot meristem, leaf petiole and also in anther
additional information
PAO3 promoter activity is detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower
expression is constitutive, but highest in flower organ
present in very young flower buds, later during flower development in pistils and anthers, especially in pistil walls and septum of young flowers. Anther filaments, pollen grains, nectar andguard cells of sepals are stained too, pollen staining persists during pollination and pollen tube growth
PAO3 promoter activity is detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower
PAO3 promoter activity is detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower
in anthers and in particular in anther tapetal cells, localized in the anther-filament junction site, localized in sepals, petals and pistils, but not in pollen grains
present very early during flower development. As flower development proceeds and before pollen maturation, strong staining appeared in pistils (stigma and ovary wall), which gradually decreases and finally disappears
additional information
isozyme AtPAO3 is abundantly expressed in all tissues
additional information
-
isozyme AtPAO3 is abundantly expressed in all tissues
additional information
expression is constitutive, but highest in flower organ. PAO3 promoter activity is detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower
additional information
expression is constitutive, but highest in flower organ. PAO3 promoter activity is detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower
additional information
-
expression is constitutive, but highest in flower organ. PAO3 promoter activity is detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower
additional information
expression pattern of AtPAO3 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO3 is mostly expressed in columella, guard cells and pollen
additional information
expression pattern of AtPAO3 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO3 is mostly expressed in columella, guard cells and pollen
additional information
expression pattern of AtPAO3 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO3 is mostly expressed in columella, guard cells and pollen
additional information
-
expression pattern of AtPAO3 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO3 is mostly expressed in columella, guard cells and pollen
additional information
expression pattern of AtPAO2 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO2 is mostly expressed in the quiescent center, columella initials and pollen
additional information
expression pattern of AtPAO2 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO2 is mostly expressed in the quiescent center, columella initials and pollen
additional information
expression pattern of AtPAO2 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO2 is mostly expressed in the quiescent center, columella initials and pollen
additional information
-
expression pattern of AtPAO2 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO2 is mostly expressed in the quiescent center, columella initials and pollen
additional information
expression pattern of AtPAO5 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO5 is mostly expressed in the vascular system of roots and hypocotyls
additional information
expression pattern of AtPAO5 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO5 is mostly expressed in the vascular system of roots and hypocotyls
additional information
expression pattern of AtPAO5 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO5 is mostly expressed in the vascular system of roots and hypocotyls
additional information
-
expression pattern of AtPAO5 during seedling and flower growth and development through analysis of promoter activity in AtPAO::GUS transgenic Arabidopsis thaliana plants. AtPAO5 is mostly expressed in the vascular system of roots and hypocotyls
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isozyme AtPAO3 contains a peroxisomal targeting motif at the C terminus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
AtPAO2-AtPAO4 form a subfamily of polyamine oxxidases different from AtPAO1, EC 1.5.3.16, overview
malfunction
loss-of-function of AtPAO gene results to increased NADPH-oxidase-dependent production of superoxide anions but not H2O2, which activates the mitochondrial alternative oxidase pathway (AOX). On the contrary, overexpression of AtPAO3 results in an increased but balanced production of both H2O2 and superoxide anions
physiological function
evolution
AtPAO2-AtPAO4 form a subfamily of polyamine oxxidases different from AtPAO1, EC 1.5.3.16, overview
malfunction
metabolism
physiological function
physiological function
pollen from mutants lacking expression of the peroxisomal-encoding AtPAO3 gene, is unable to induce the opening of the Ca2+-permeable channels in the presence of spermidine, resulting in reduced pollen tube growth and seed number. A high spermidine concentration triggers a Ca2+ influx beyond the optimal, which has adeleterious effect
physiological function
plant PAOs oxidize the carbon at the endo-side of the N4-nitrogen of Spd and Spm, producing 4-aminobutanal and N-(3-aminopropyl)-4-aminobutanal, respectively, in addition to 1,3-diaminopropane and H2O2, and are considered to be involved in terminal catabolism of polyamines, physiological role(s) of the polyamine catabolic pathways in plants, overview. All AtPAOs characterized are involved in a polyamine backconversion pathway
physiological function
the cross-talk of the enzyme with NADPH-oxidase balances intracellular superoxide anion/H2O2 which in turn affects the cytochrome-c pathway/alternative terminal oxidase pathway
malfunction
loss-of-function mutants contain 2-fold higher thermospermine levels and exhibit delayed transition from vegetative to reproductive growth compared with that of wild-type plants
malfunction
two loss-of-function atpao5 mutants and a 35S::AtPAO5 Arabidopsis transgenic line present phenotypical differences from the wild-type plants with regard to stem and root elongation, differences that are accompanied by changes in polyamine levels and the number of xylem vessels. It is shown that cytokinin treatment, which up-regulates AtPAO5 expression in roots, differentially affects protoxylem differentiation in 35S::AtPAO5, atpao5, and wild-type roots
metabolism
the enzyme is involved in the polyamine back-conversion pathway, overview
metabolism
the enzyme contributes to abscisic acid mediated plant developmental processes
physiological function
plant PAOs oxidize the carbon at the endo-side of the N4-nitrogen of Spd and Spm, producing 4-aminobutanal and N-(3-aminopropyl)-4-aminobutanal, respectively, in addition to 1,3-diaminopropane and H2O2, and are considered to be involved in terminal catabolism of polyamines, physiological role(s) of the polyamine catabolic pathways in plants, overview. All AtPAOs characterized are involved in a polyamine backconversion pathway
physiological function
polyaminehomeostasis, plant growth, stress response
physiological function
potential contributory function of the enzyme AtPAO2 in NO-mediated effects on root growth
physiological function
the enzyme has a function in abscisic acid modulating vegetative growth and in root architecture
physiological function
the enzyme is a source of H2O2 generation in Arabidopsis guard cells and plays crucial roles in stomatal movement
physiological function
the enzyme is involved in the control of Therm-Spm homeostasis. It participates in the tightly controlled interplay between auxin and cytokinins that is necessary for proper xylem differentiation
physiological function
the enzyme regulates thermospermine homeostasis through a thermospermine oxidation pathway
physiological function
isoforms Pao1 and Pao2 single mutant lines display altered responses to Pseudomonas syringae, and an increased susceptibility is found in the Pao1/Pao2 double mutant. These mutant lines show disturbed contents of ROS (H2O2 and O2- radical) and altered activities of superoxide dismutase, catalase and respiratory burst oxidase homologue enzymes both in infected and control plants
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PAO3_ARATH
488
0
54132
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54100
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
homozygous lines of T-DNA insertional mutant of Arabidopsis thaliana SALK_121288 for the AtPAO3 gene
additional information
homozygous lines of T-DNA insertional mutant of Arabidopsis thaliana SALK_121288 for the AtPAO3 gene
additional information
homozygous lines of T-DNA insertional mutant of Arabidopsis thaliana SALK_121288 for the AtPAO3 gene
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant AtPAO3 fused to the maltose-binding protein from Escherichia coli
recombinant maltose-binding protein fusion enzyme from Escherichia coli by amylose affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtPAO3, DNA and amino acid sequence determination and analysis, intron/exon organization, sequence comparisons, recombinant expression as maltose-binding protein fusion protein in Escherichia coli, and expression of GFP-tagged AtPAO3 in transgenic Arabidopsis thaliana plants using the Agrobacterium tumefaciens (strain C58C1)-mediated floral dip transformation method resulting in increased putrescine levels after feeding of exogenous spermidine
AtPAO3, expression as GFP-tagged enzyme in plant cells, expression of AtPAO3 fused to the maltose-binding protein in Escherichia coli strain BL21 in a temperature-dependent manner, overview
gene AtPAO3, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants
transient expression of isozyme AtPAO3 in Arabidopsis thaliana root cell peroxisomes as monomeric red fluorescent protein fusion protein
AtPAO2, DNA and amino acid sequence determination and analysis, intron/exon organization, sequence comparisons, expression of His6-tagged enzyme in Escherichia coli, expression of GFP-tagged AtPAO3 in Arabidopsis thaliana plants using the Agrobacterium tumefaciens (strain C58C1)-mediated floral dip transformation method
AtPAO4, DNA and amino acid sequence determination and analysis, intron/exon organization, sequence comparisons, expression of His6-tagged enzyme in Escherichia coli, expression of GFP-tagged AtPAO3 in Arabidopsis thaliana plants using the Agrobacterium tumefaciens (strain C58C1)-mediated floral dip transformation method
gene AtPAO2, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants
gene AtPAO5, construction of AtPAO::GUS transgenic Arabidopsis thaliana plants
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AtPAO3 mRNA rapidly accumulats in wounded plants 1 h after wounding and returns to almost basal levels 6 h thereafter. Seedlings treated with flagellin 22, a pathogen elicitor that activates the plant basal defense, exhibits AtPAO3 induction after the 6-h time point, with constant increase up to 24 h
AtPAO2 uORF has a regulatory role in regulating AtPAO2 expression. The fact that uORFs are commonly found in plant polyamine oxidase genes is relevant, implying that regulatory elements in the 5'-UTR of polyamine biosynthetic and catabolic genes might finely control the intracellular concentration of polyamines in plant development and stress responses
isoforms PAO1 and PAO2 genes are transcriptionally up-regulated in plants infected by Pseudomonas syringae
NO3- induced AtPAO2::GUS expression is quenched by the presence of NH4+ in the growth medium and abscisic acid-induced AtPAO2::GUS expression is more prominent when the plants are grown on NO3- as the only N source. PAO2OX (an AtPAO2 over-expressing transgenic line) is partially unresponsive to abscisic acid in some growth conditions depending on N-source, pao2 mutants being often more sensitive to abscisic acid than the similarly grown WT
NO3- induced AtPAO2::GUS expression is quenched by the presence of NH4+ in the growth medium and abscisic acid-induced AtPAO2::GUS expression was more prominent when the plants are grown on NO3- as the only N source
positive regulation of AtPAO5 expression by polyamines at the transcriptional and post-transcriptional level
the peptide derived from the AtPAO2 uORF is necessary for translational regulation of the AtPAO2 mORF
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kamada-Nobusada, T.; Hayashi, M.; Fukazawa, M.; Sakakibara, H.; Nishimura, M.
A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine catabolism in Arabidopsis thaliana
Plant Cell Physiol.
49
1272-1282
2008
Arabidopsis thaliana (Q9LYT1), Arabidopsis thaliana
Moschou, P.N.; Sanmartin, M.; Andriopoulou, A.H.; Rojo, E.; Sanchez-Serrano, J.J.; Roubelakis-Angelakis, K.A.
Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis
Plant Physiol.
147
1845-1857
2008
Arabidopsis thaliana (Q9LYT1)
Fincato, P.; Moschou, P.N.; Spedaletti, V.; Tavazza, R.; Angelini, R.; Federico, R.; Roubelakis-Angelakis, K.A.; Tavladoraki, P.
Functional diversity inside the Arabidopsis polyamine oxidase gene family
J. Exp. Bot.
6
1155-1168
2010
Arabidopsis thaliana (Q9LYT1), Arabidopsis thaliana (Q9SKX5), Arabidopsis thaliana
Takahashi, Y.; Cong, R.; Sagor, G.H.; Niitsu, M.; Berberich, T.; Kusano, T.
Characterization of five polyamine oxidase isoforms in Arabidopsis thaliana
Plant Cell Rep.
29
955-965
2010
Arabidopsis thaliana (Q9LYT1), Arabidopsis thaliana (Q9SKX5), Arabidopsis thaliana
Wu, J.; Shang, Z.; Wu, J.; Jiang, X.; Moschou, P.N.; Sun, W.; Roubelakis-Angelakis, K.A.; Zhang, S.
Spermidine oxidase-derived H2O2 regulates pollen plasma membrane hyperpolarization-activated Ca(2+)-permeable channels and pollen tube growth
Plant J.
63
1042-1053
2010
Arabidopsis thaliana (Q9LYT1)
Fincato, P.; Moschou, P.N.; Ahou, A.; Angelini, R.; Roubelakis-Angelakis, K.A.; Federico, R.; Tavladoraki, P.
The members of Arabidopsis thaliana PAO gene family exhibit distinct tissue- and organ-specific expression pattern during seedling growth and flower development
Amino Acids
42
831-841
2012
Arabidopsis thaliana (Q9LYT1), Arabidopsis thaliana (Q9SKX5), Arabidopsis thaliana (Q9SU79), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9LYT1), Arabidopsis thaliana Col-0 (Q9SKX5), Arabidopsis thaliana Col-0 (Q9SU79)
Fincato, P.; Moschou, P.N.; Spedaletti, V.; Tavazza, R.; Angelini, R.; Federico, R.; Roubelakis-Angelakis, K.A.; Tavladoraki, P.
Functional diversity inside the Arabidopsis polyamine oxidase gene family
J. Exp. Bot.
62
1155-1168
2011
Arabidopsis thaliana, Arabidopsis thaliana (Q9LYT1), Arabidopsis thaliana (Q9SKX5), Arabidopsis thaliana Columbia-0, Arabidopsis thaliana Columbia-0 (Q9LYT1), Arabidopsis thaliana Columbia-0 (Q9SKX5)
Andronis, E.A.; Moschou, P.N.; Toumi, I.; Roubelakis-Angelakis, K.A.
Peroxisomal polyamine oxidase and NADPH-oxidase cross-talk for ROS homeostasis which affects respiration rate in Arabidopsis thaliana
Front. Plant Sci.
5
132
2014
Arabidopsis thaliana (Q9LYT1), Arabidopsis thaliana
Tavladoraki, P.; Cona, A.; Angelini, R.
Copper-containing amine oxidases and FAD-dependent polyamine oxidases are key players in plant tissue differentiation and organ development
Front. Plant Sci.
7
824
2016
Arabidopsis thaliana (Q9FNA2), Arabidopsis thaliana (Q9SU79)
-
Ahou, A.; Martignago, D.; Alabdallah, O.; Tavazza, R.; Stano, P.; Macone, A.; Pivato, M.; Masi, A.; Rambla, J.L.; Vera-Sirera, F.; Angelini, R.; Federico, R.; Tavladoraki, P.
A plant spermine oxidase/dehydrogenase regulated by the proteasome and polyamines
J. Exp. Bot.
65
1585-1603
2014
Arabidopsis thaliana (Q9SU79)
Alabdallah, O.; Ahou, A.; Mancuso, N.; Pompili, V.; Macone, A.; Pashkoulov, D.; Stano, P.; Cona, A.; Angelini, R.; Tavladoraki, P.
The Arabidopsis polyamine oxidase/dehydrogenase 5 interferes with cytokinin and auxin signaling pathways to control xylem differentiation
J. Exp. Bot.
68
997-1012
2017
Arabidopsis thaliana (Q9SU79)
Hou, Z.; Liu, G.; Hou, L.; Wang, L.; Liu, X.
Regulatory function of polyamine oxidase-generated hydrogen peroxide in ethylene-induced stomatal closure in Arabidopsis thaliana
J. Integr. Agric.
12
251-262
2013
Arabidopsis thaliana (Q9SKX5)
-
Guerrero-Gonzalez, M.L.; Rodriguez-Kessler, M.; Jimenez-Bremont, J.F.
uORF, a regulatory mechanism of the Arabidopsis polyamine oxidase 2
Mol. Biol. Rep.
41
2427-2443
2014
Arabidopsis thaliana (Q9SKX5)
Kim, D.W.; Watanabe, K.; Murayama, C.; Izawa, S.; Niitsu, M.; Michael, A.J.; Berberich, T.; Kusano, T.
Polyamine oxidase 5 regulates Arabidopsis growth through Thermospermine oxidase activity
Plant Physiol.
165
1575-1590
2014
Arabidopsis thaliana (Q9SU79)
Guerrero-Gonzalez, M.L.; Ortega-Amaro, M.A.; Juarez-Montiel, M.; Jimenez-Bremont, J.F.
Arabidopsis Polyamine oxidase-2 uORF is required for downstream translational regulation
Plant Physiol. Biochem.
108
381-390
2016
Arabidopsis thaliana (Q9SKX5), Arabidopsis thaliana
Wimalasekera, R.; Schaarschmidt, F.; Angelini, R.; Cona, A.; Tavladoraki, P.; Scherer, G.F.
Polyamine oxidase 2 of Arabidopsis contributes to ABA mediated plant developmental processes
Plant Physiol. Biochem.
96
231-240
2015
Arabidopsis thaliana (Q9SKX5)
Jasso-Robles, F.; Gonzalez, M.; Pieckenstain, F.; Ramixadrez-Garcixada, J.; Guerrero-Gonzalez, M.; Jimenez-Bremont, J.; Rodriguez-Kessler, M.
Decrease of Arabidopsis PAO activity entails increased RBOH activity, ROS content and altered responses to Pseudomonas
Plant Sci.
292
110372
2020
Arabidopsis thaliana (Q9FNA2), Arabidopsis thaliana (Q9SKX5), Arabidopsis thaliana
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