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N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
norspermine + O2 + H2O
? + H2O2
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
thermospermine + O2 + H2O
? + H2O2
thermospermine + O2 + H2O
norspermidine + ?
-
-
-
?
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 + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
-
-
-
?
norspermine + O2 + H2O
? + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
thermospermine + O2 + H2O
?
thermospermine + O2 + H2O
? + H2O2
additional information
?
-
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
less than 10% of the activity with norspermine
-
-
?
norspermine + O2 + H2O
?
-
-
-
?
norspermine + O2 + H2O
?
-
-
-
?
norspermine + O2 + H2O
? + H2O2
-
-
-
?
norspermine + O2 + H2O
? + H2O2
best substrate
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
enzyme is involved in a polyamine back-conversion pathway
-
-
?
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
about 20% of the activity with norspermine
-
-
?
thermospermine + O2 + H2O
? + H2O2
-
-
-
?
thermospermine + O2 + H2O
? + H2O2
about 65% of the activity with norspermine
-
-
?
norspermine + O2 + H2O
?
-
-
-
-
?
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
-
-
?
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
AtPAO4 specifically catalyzes the conversion of spermine to spermidine under the assay conditions
-
-
?
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, substratr 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 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
bets substrate
-
-
?
thermospermine + O2 + H2O
?
-
-
-
-
?
thermospermine + O2 + H2O
?
-
-
-
?
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
-
-
-
?
thermospermine + O2 + H2O
? + H2O2
about 10% of the activity with spermine
-
-
?
additional information
?
-
no activity with spermidine
-
-
?
additional information
?
-
no substrate: spermidine. 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
?
-
no substrate: spermidine. 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
?
-
-
no substrate: spermidine. 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
?
-
no activity with spermidine
-
-
?
additional information
?
-
-
no oxidation activity with spermidine
-
-
?
additional information
?
-
-
no oxidation activity with spermidine
-
-
?
additional information
?
-
AtPAO4 deficiency induces alterations in the expression of genes related to the drought stress response and flavonoid biosynthesis
-
-
?
additional information
?
-
no activity with putrescine, spermidine, N1-acetylspermine
-
-
?
additional information
?
-
peroxisomal polyamine oxidase AtPAO4 is involved in the catabolism of polyamines in leaves, overview
-
-
?
additional information
?
-
no substrate: spermidine, N1-acetylspermine, norspermine
-
-
?
additional information
?
-
no substrate: spermidine, N1-acetylspermine, norspermine
-
-
?
additional information
?
-
-
no substrate: spermidine, N1-acetylspermine, norspermine
-
-
?
additional information
?
-
spermidine is oxidized with very low efficiency. 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
?
-
spermidine is oxidized with very low efficiency. 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
?
-
-
spermidine is oxidized with very low efficiency. 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
-
-
?
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0.02
thermospermine
pH 8.0, temperature not specified in the publication
0.47
N1-acetylspermine
-
pH 8.0, 25°C, recombinant AtPAO1
6.9
norspermine
-
pH 8.0, 25°C, recombinant AtPAO1
5.7
thermospermine
-
pH 8.0, 25°C, recombinant AtPAO1
additional information
additional information
-
Michaelis-Menten kinetics
-
0.47
N1-acetylspermine
pH 8.0
0.47
N1-acetylspermine
pH 8.0, temperature not specified in the publication
0.09
norspermine
pH 8.0
0.9
norspermine
pH 8.0, temperature not specified in the publication
0.11
spermine
pH 8.0
0.12
spermine
pH 8.0, temperature not specified in the publication
0.0046
O2
pH 7.5, 25°C, cosubstrate: N1-acetylspermine
0.0051
O2
pH 7.5, 25°C, cosubstrate: thermospermine
11
O2
pH 7.5, 25°C, cosubstrate: spermine
0.0256
spermine
37°C, pH 7.5
0.047
spermine
pH 7.5, temperature not specified in the publication
0.0787
spermine
37°C, pH 6.5
0.12
spermine
-
pH 8.0, 25°C, recombinant AtPAO1
0.23
spermine
recombinant His-tagged isozyme AtPAO4
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Tavladoraki, P.; Rossi, M.N.; Saccuti, G.; Perez-Amador, M.A.; Polticelli, F.; Angelini, R.; Federico, R.
Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion
Plant Physiol.
141
1519-1532
2006
Arabidopsis thaliana (Q9FNA2)
brenda
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 (Q8H191)
brenda
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 (Q8H191), Arabidopsis thaliana (Q9FNA2), Arabidopsis thaliana
brenda
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 (Q8H191), Arabidopsis thaliana (Q9FNA2), Arabidopsis thaliana
brenda
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
brenda
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 Columbia-0
brenda
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 (Q8H191), Arabidopsis thaliana (Q9FNA2)
brenda
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)
brenda
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 (Q8H191)
-
brenda
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)
brenda