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(3R,3'R)-dimethylspermine + 2 O2 + 2 H2O
putrescine + 2 3-aminobutanal + 2 H2O2
-
-
-
-
?
(3S,3'S)-dimethylspermine + 2 O2 + 2 H2O
putrescine + 2 3-aminobutanal + 2 H2O2
-
-
-
-
?
benzylamidine + O2 + H2O
?
-
-
-
-
?
N,N'-bis(3-aminopropyl)ethylenediamine + O2 + H2O
?
-
-
-
-
?
N,N'-dibenzyl-1,4-diaminobutane + O2 + H2O
? + H2O2
-
slow substrate
-
-
?
N1-acetylspermidine + O2 + H2O
?
weak activity
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
norspermidine + O2 + H2O
?
-
-
-
-
?
norspermine + O2 + H2O
? + H2O2
spermidine + O2 + H2O
?
-
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminobutanal + H2O2
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
thermospermine + O2 + H2O
?
thermospermine + O2 + H2O
? + H2O2
thermospermine + O2 + H2O
norspermidine + 3-acetamidopropanal + H2O2
thermospermine + O2 + H2O
norspermidine + ?
thermospermine + O2 + H2O
spermidine + ?
tryptamine + O2 + H2O
?
-
-
-
-
?
additional information
?
-
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
?
weak activity
-
-
?
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
?
-
-
-
-
?
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-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
at pH 8.0, the substrate preference in decreasing order is as follows: spermine / thermospermine, N1-acetylspermine, norspermine, spermidine. At pH 7.0, the substrate preference in decreasing order is as follows: thermospermine, norspermine, spermine, N1-acetylspermine, spermidine
-
-
?
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
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
-
-
?
norspermine + O2 + H2O
?
-
-
-
?
norspermine + O2 + H2O
?
-
-
-
?
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
?
-
-
-
?
norspermine + O2 + H2O
?
-
-
-
-
?
norspermine + O2 + H2O
?
-
the recombinant OsPAO1 enzyme prefers therospermine as a substrate at pH 6.0 and spermine at pH 8.5
-
-
?
norspermine + O2 + H2O
?
-
the recombinant OsPAO1 enzyme prefers therospermine as a substrate at pH 6.0 and spermine at pH 8.5
-
-
?
norspermine + O2 + H2O
?
at pH 8.0, the substrate preference in decreasing order is as follows: spermine / thermospermine, N1-acetylspermine, norspermine, spermidine. At pH 7.0, the substrate preference in decreasing order is as follows: thermospermine, norspermine, spermine, N1-acetylspermine, spermidine
-
-
?
norspermine + O2 + H2O
? + H2O2
-
-
-
?
norspermine + O2 + H2O
? + H2O2
about 40% of the activity with spermidine
-
-
?
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-aminobutanal + H2O2
-
-
-
?
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
-
-
?
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
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
-
-
-
?
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
reaction is catalyzed at very low rates (at pH 7.0 and at pH 8.0). At pH 8.0, the substrate preference in decreasing order is as follows: spermine / thermospermine, N1-acetylspermine, norspermine, spermidine. At pH 7.0, the substrate preference in decreasing order is as follows: thermospermine, norspermine, spermine, N1-acetylspermine, spermidine
-
-
?
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
-
-
-
?
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 + 3-aminopropanal + H2O2
-
-
-
?
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
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
slow substrate
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
the recombinant OsPAO1 enzyme prefers therospermine as a substrate at pH 6.0 and spermine at pH 8.5
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
the recombinant OsPAO1 enzyme prefers therospermine as a substrate at pH 6.0 and spermine at pH 8.5
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
at pH 8.0, the substrate preference in decreasing order is as follows: spermine / thermospermine, N1-acetylspermine, norspermine, spermidine. At pH 7.0, the substrate preference in decreasing order is as follows: thermospermine, norspermine, spermine, N1-acetylspermine, spermidine
-
-
?
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
?
-
-
-
?
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
?
-
-
-
-
?
thermospermine + O2 + H2O
?
-
the recombinant OsPAO1 enzyme prefers therospermine as a substrate at pH 6.0 and spermine at pH 8.5
-
-
?
thermospermine + O2 + H2O
?
-
the recombinant OsPAO1 enzyme prefers therospermine as a substrate at pH 6.0 and spermine at pH 8.5
-
-
?
thermospermine + O2 + H2O
? + H2O2
-
-
-
?
thermospermine + O2 + H2O
? + H2O2
about 30% of the activity with spermidine
-
-
?
thermospermine + O2 + H2O
norspermidine + 3-acetamidopropanal + H2O2
-
-
-
?
thermospermine + O2 + H2O
norspermidine + 3-acetamidopropanal + H2O2
norspermidine is generated via thermospermine catabolism in Selaginella lepidophylla
-
-
?
thermospermine + O2 + H2O
norspermidine + ?
-
-
-
?
thermospermine + O2 + H2O
norspermidine + ?
at pH 8.0, the substrate preference in decreasing order is as follows: spermine / thermospermine, N1-acetylspermine, norspermine, spermidine. At pH 7.0, the substrate preference in decreasing order is as follows: thermospermine, norspermine, spermine, N1-acetylspermine, 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 spermidine
-
-
?
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
?
-
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
-
-
?
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
?
-
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
?
-
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
?
-
-
N-acetylated polyamines and diamines, e.g. N1-acetylspermidine, N8-acetylspermidine, N-acetylspermine, N1,N12-diacetylspermine, putrescine, cadaverine and histamine, are not accepted as substrates. Bis(benzyl)polyamines, such as MDL 27695 and MDL 27391, are not substrates
-
-
?
additional information
?
-
-
Bjpao1 shows no activity with N1-acetylspermine
-
-
?
additional information
?
-
Bjpao1 shows no activity with N1-acetylspermine
-
-
?
additional information
?
-
-
Bjpao2 shows no activity with spermine
-
-
?
additional information
?
-
Bjpao2 shows no activity with spermine
-
-
?
additional information
?
-
flavoprotein oxidase Fms1 catalyzes the oxidation of spermine and N1-acetylspermine to spermidine and 3-aminopropanal or N-acetyl-3-aminopropanal
-
-
?
additional information
?
-
-
Fms1 prefers (S,S)- to (R,R)-diastereoisomer, but with notably lower kcat in comparison with spermine. Fms1 is prone to aldehyde supplementation in its regioselectivity, i.e. the cleavage site of spermidine
-
-
-
additional information
?
-
substrate preference in decreasing order: spermine, spermidine, N1-acetylspermine
-
-
-
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0.098
(3R,3'R)-dimethylspermine
-
pH 7.4, 25°C
-
0.061
(3S,3'S)-dimethylspermine
-
pH 7.4, 25°C
-
1.6
benzylamidine
-
pH 8.5, 37°C
1.898
N,N'-bis(3-aminopropyl)ethylenediamine
-
pH 7.2, 37°C
0.027 - 0.37
N,N'-dibenzyl-1,4-diaminobutane
0.042 - 1
N1-acetylspermidine
0.0019 - 2.125
N1-acetylspermine
5
norspermidine
-
pH 8.5, 37°C
0.0037 - 0.05
thermospermine
2.5
tryptamine
-
pH 8.5, 37°C
additional information
additional information
-
0.027
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant wild-type enzyme
0.13
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant mutant H64Q
0.27
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant mutant H64A
0.37
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant mutant H64N
0.042
N1-acetylspermidine
pH 7.5, 37°C, recombinant AtPAO3
1
N1-acetylspermidine
37°C, pH 7.0
0.0019
N1-acetylspermine
37°C, pH 7.5
0.011
N1-acetylspermine
pH 9.0, 25°C, recombinant wild-type Fms1
0.02
N1-acetylspermine
pH 7.5, 37°C, recombinant AtPAO3
0.0218
N1-acetylspermine
37°C, pH 6.5
0.03
N1-acetylspermine
pH 9.0, 25°C, recombinant mutant D94N
0.0359
N1-acetylspermine
-
pH 8.5, 30°C
0.0369
N1-acetylspermine
37°C, pH 8.0, wild-type enzyme
0.043
N1-acetylspermine
37°C, pH 8.0, mutant enzyme K315M
0.046
N1-acetylspermine
37°C, pH 8.0, mutant enzyme T467Y
0.05
N1-acetylspermine
-
pH 10.0, 30°C, recombinant mutant H64A
0.053
N1-acetylspermine
-
pH 10.0, 30°C, recombinant mutant H64Q
0.058
N1-acetylspermine
37°C, pH 8.0, mutant enzyme T467S
0.062
N1-acetylspermine
37°C, pH 8.0, mutant enzyme H69E
0.071
N1-acetylspermine
37°C, pH 8.0, mutant enzyme H69Q
0.104
N1-acetylspermine
pH 9.0, 25°C, recombinant mutant N195A
0.21
N1-acetylspermine
-
pH 10.0, 30°C, recombinant wild-type enzyme
0.233
N1-acetylspermine
pH 7.5, temperature not specified in the publication
0.233
N1-acetylspermine
pH 7.5, 25°C, recombinant AtPAO2
0.24
N1-acetylspermine
-
pH 10.0, 30°C, recombinant mutant H64N
2
N1-acetylspermine
37°C, pH 7.0
2
N1-acetylspermine
pH 7.5, temperature not specified in the publication
2
N1-acetylspermine
pH 7.5, 25°C, recombinant AtPAO3
2.125
N1-acetylspermine
-
pH 7.2, 37°C
0.011
norspermine
-
pH 6.0, 30°C
0.0145
norspermine
-
pH 8.5, 30°C
0.0158
norspermine
37°C, pH 6.5
0.0255
norspermine
37°C, pH 7.5
0.045
norspermine
pH 7.5, temperature not specified in the publication
0.045
norspermine
pH 7.5, 25°C, recombinant AtPAO3
2
norspermine
-
pH 8.5, 37°C
0.0046
O2
pH 7.5, 25°C, cosubstrate: N1-acetylspermine
0.0051
O2
pH 7.5, 25°C, cosubstrate: thermospermine
0.015
O2
pH 9.0, 25°C, recombinant mutant N195A, with spermine
0.02
O2
pH 9.0, 25°C, recombinant mutant N195A, with N1-acetylspermine
0.0436
O2
pH 9.0, 25°C, recombinant wild-type Fms1, with N1-acetylspermine
0.07
O2
-
pH 10.0, 30°C, recombinant wild-type enzyme, with spermine
0.091
O2
pH 9.0, 25°C, recombinant wild-type Fms1, with spermine
0.097
O2
pH 9.0, 25°C, recombinant mutant D94N, with N1-acetylspermine
0.15
O2
-
pH 8.6, 30°C, recombinant mutants H64A and H64Q, with N,N'-dibenzyl-1,4-diaminobutane
0.16
O2
-
pH 8.6, 30°C, recombinant wild-type enzyme, with N,N'-dibenzyl-1,4-diaminobutane
0.192
O2
pH 9.0, 25°C, recombinant mutant D94N, with spermine
0.2
O2
-
pH 8.6, 30°C, recombinant mutant H64N, with N,N'-dibenzyl-1,4-diaminobutane
0.3
O2
-
pH 10.0, 30°C, recombinant mutants H64A and H64N, with spermine
0.5
O2
-
pH 10.0, 30°C, recombinant mutant H64Q, with spermine
11
O2
pH 7.5, 25°C, cosubstrate: spermine
39
O2
-
pH 10.0, 30°C, recombinant wild-type enzyme and recombinant mutants H64A and H64N, with N1-acetylspermine
53
O2
-
pH 10.0, 30°C, recombinant mutant H64Q, with N1-acetylspermine
0.007
spermidine
37°C, pH 9.5, wild-type enzyme
0.0124
spermidine
37°C, pH 9.5, wild-type enzyme
0.016
spermidine
37°C, pH 9.5, mutant enzyme K301M
0.017
spermidine
37°C, pH 9.5, mutant enzyme T460Y
0.019
spermidine
37°C, pH 9.5, mutant enzyme H64E
0.019
spermidine
37°C, pH 9.5, mutant enzyme T460S
0.02
spermidine
37°C, pH 9.5, mutant enzyme T467Y
0.021
spermidine
37°C, pH 9.5, mutant enzyme H64Q
0.0229
spermidine
37°C, pH 9.5, mutant enzyme H69Q
0.025
spermidine
37°C, pH 9.5, mutant enzyme H69E
0.031
spermidine
37°C, pH 9.5, mutant enzyme K315M
0.0683
spermidine
37°C, pH 7.5
0.139
spermidine
pH 7.5, 25°C, recombinant AtPAO4
0.182
spermidine
37°C, pH 9.5, mutant enzyme T467S
0.204
spermidine
37°C, pH 7.0
0.204
spermidine
pH 7.5, 37°C, recombinant AtPAO3
0.274
spermidine
pH 7.5, temperature not specified in the publication
0.274
spermidine
pH 7.5, 25°C, recombinant AtPAO3
0.409
spermidine
pH 7.5, temperature not specified in the publication
0.409
spermidine
pH 7.5, 25°C, recombinant AtPAO2
0.456
spermidine
pH 8.5, 30°C
0.66
spermidine
-
pH 8.5, 37°C
2.34
spermidine
-
pH 7.2, 37°C
0.0049
spermine
-
pH 6.0, 30°C
0.0061
spermine
-
pH 8.5, 30°C
0.00836
spermine
37°C, pH 8.5, wild-type enzyme
0.012
spermine
37°C, pH 8.5, mutant enzyme T460S
0.013
spermine
37°C, pH 8.5, mutant enzyme T460Y
0.017
spermine
37°C, pH 8.5, mutant enzyme K301M
0.024
spermine
37°C, pH 8.5, mutant enzyme H64E
0.0256
spermine
37°C, pH 7.5
0.0269
spermine
37°C, pH 8.5, mutant enzyme H64Q
0.04
spermine
-
pH 10.0, 30°C, recombinant mutant H64N
0.047
spermine
pH 7.5, 25°C, recombinant AtPAO4
0.077
spermine
-
pH 7.4, 25°C
0.0787
spermine
37°C, pH 6.5
0.098
spermine
pH 8.5, 30°C
0.118
spermine
pH 9.35, 25°C, recombinant wild-type Fms1
0.127
spermine
pH 9.35, 25°C, recombinant mutant N195A
0.16
spermine
-
pH 10.0, 30°C, recombinant wild-type enzyme
0.21
spermine
-
pH 10.0, 30°C, recombinant mutants H64A and H64Q
0.211
spermine
-
pH 7.2, 37°C
0.27
spermine
pH 7.5, temperature not specified in the publication
0.27
spermine
pH 7.5, 25°C, recombinant AtPAO2
0.32
spermine
pH 9.35, 25°C, recombinant mutant D94N
0.35
spermine
-
pH 8.5, 37°C
0.58
spermine
pH 7.5, temperature not specified in the publication
0.58
spermine
pH 7.5, 25°C, recombinant AtPAO3
0.588
spermine
37°C, pH 7.0
0.588
spermine
pH 7.5, 37°C, recombinant AtPAO3
0.0037
thermospermine
-
pH 6.0, 30°C
0.0051
thermospermine
37°C, pH 7.5
0.0137
thermospermine
37°C, pH 6.5
0.05
thermospermine
pH 7.5, temperature not specified in the publication
0.05
thermospermine
pH 7.5, 25°C, recombinant AtPAO3
additional information
additional information
-
steady-state 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
seady-state kinetics and rapid-reaction kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
steady-state kinetics and rapid-reaction kinetics of wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.77
(3R,3'R)-dimethylspermine
-
pH 7.4, 25°C
-
1.85
(3S,3'S)-dimethylspermine
-
pH 7.4, 25°C
-
0.16 - 0.9
N,N'-dibenzyl-1,4-diaminobutane
0.042 - 1
N1-acetylspermidine
0.014 - 49
N1-acetylspermine
0.035 - 0.5
thermospermine
0.16
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant mutant H64A
0.2
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant mutant H64Q
0.22
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant mutant H64N
0.9
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant wild-type enzyme
0.042
N1-acetylspermidine
37°C, pH 7.0
1
N1-acetylspermidine
pH 7.5, 37°C, recombinant AtPAO3
0.014
N1-acetylspermine
pH 7.5, 25°C, recombinant AtPAO4
0.02
N1-acetylspermine
37°C, pH 7.0
0.02
N1-acetylspermine
pH 7.5, temperature not specified in the publication
0.02
N1-acetylspermine
pH 7.5, 25°C, recombinant AtPAO3
0.022
N1-acetylspermine
-
pH 8.5, 30°C
0.025
N1-acetylspermine
37°C, pH 6.5
0.084
N1-acetylspermine
37°C, pH 7.5
0.8
N1-acetylspermine
pH 7.5, temperature not specified in the publication
0.8
N1-acetylspermine
pH 7.5, 25°C, recombinant AtPAO2
2
N1-acetylspermine
pH 7.5, 37°C, recombinant AtPAO3
3.1
N1-acetylspermine
-
pH 10.0, 30°C, recombinant mutant H64A
4.1
N1-acetylspermine
-
pH 10.0, 30°C, recombinant mutant H64N
4.5
N1-acetylspermine
-
pH 10.0, 30°C, recombinant mutant H64Q
8.1
N1-acetylspermine
pH 9.0, 25°C, recombinant mutant N195A
9.7
N1-acetylspermine
pH 9.0, 25°C, recombinant mutant D94N
15.1
N1-acetylspermine
pH 9.0, 25°C, recombinant wild-type Fms1
49
N1-acetylspermine
-
pH 10.0, 30°C, recombinant wild-type enzyme
0.012
norspermine
37°C, pH 6.5
0.018
norspermine
-
pH 6.0, 30°C
0.036
norspermine
-
pH 8.5, 30°C
0.086
norspermine
37°C, pH 7.5
0.45
norspermine
pH 7.5, 25°C, recombinant AtPAO4
1.1
norspermine
pH 7.5, temperature not specified in the publication
1.1
norspermine
pH 7.5, 25°C, recombinant AtPAO3
2.9
norspermine
pH 7.5, temperature not specified in the publication
2.9
norspermine
pH 7.5, 25°C, recombinant AtPAO2
0.009
spermidine
37°C, pH 7.5
0.1
spermidine
pH 7.5, 25°C, recombinant AtPAO4
0.17
spermidine
pH 8.5, 30°C
1.25
spermidine
37°C, pH 7.0
1.25
spermidine
pH 7.5, 37°C, recombinant AtPAO3
3.4
spermidine
pH 7.5, temperature not specified in the publication
3.4
spermidine
pH 7.5, 25°C, recombinant AtPAO3
4.6
spermidine
pH 7.5, temperature not specified in the publication
4.6
spermidine
pH 7.5, 25°C, recombinant AtPAO2
0.009
spermine
37°C, pH 6.5
0.025
spermine
-
pH 6.0, 30°C
0.043
spermine
-
pH 8.5, 30°C
0.069
spermine
37°C, pH 7.5
0.12
spermine
-
pH 10.0, 30°C, recombinant mutant H64N
0.188
spermine
37°C, pH 7.0
0.188
spermine
pH 7.5, 37°C, recombinant AtPAO3
0.3
spermine
-
pH 10.0, 30°C, recombinant mutant H64A
0.31
spermine
pH 8.5, 30°C
0.34
spermine
-
pH 10.0, 30°C, recombinant mutant H64Q
1.7
spermine
pH 7.5, temperature not specified in the publication
1.7
spermine
pH 7.5, 25°C, recombinant AtPAO3
2
spermine
pH 9.35, 25°C, recombinant mutant D94N
4.2
spermine
pH 7.5, temperature not specified in the publication
4.2
spermine
pH 7.5, 25°C, recombinant AtPAO2
4.6
spermine
pH 7.5, 25°C, recombinant AtPAO4
4.7
spermine
-
pH 10.0, 30°C, recombinant wild-type enzyme
4.9
spermine
pH 9.35, 25°C, recombinant mutant N195A
31.1
spermine
-
pH 7.4, 25°C
39
spermine
pH 9.35, 25°C, recombinant wild-type Fms1
0.035
thermospermine
37°C, pH 6.5
0.051
thermospermine
-
pH 6.0, 30°C
0.1
thermospermine
pH 7.5, 25°C, recombinant AtPAO4
0.115
thermospermine
37°C, pH 7.5
0.4
thermospermine
pH 7.5, temperature not specified in the publication
0.4
thermospermine
pH 7.5, 25°C, recombinant AtPAO2
0.5
thermospermine
pH 7.5, temperature not specified in the publication
0.5
thermospermine
pH 7.5, 25°C, recombinant AtPAO3
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.9
(3R,3'R)-dimethylspermine
-
pH 7.4, 25°C
-
30
(3S,3'S)-dimethylspermine
-
pH 7.4, 25°C
-
0.6 - 33
N,N'-dibenzyl-1,4-diaminobutane
0.01 - 1400
N1-acetylspermine
2.6 - 23.3
thermospermine
0.6
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant mutants H64A and H64N
1.6
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant mutant H64Q
33
N,N'-dibenzyl-1,4-diaminobutane
-
pH 8.6, 30°C, recombinant wild-type enzyme
0.01
N1-acetylspermine
pH 7.5, temperature not specified in the publication
0.61
N1-acetylspermine
-
pH 8.5, 30°C
3.4
N1-acetylspermine
pH 7.5, temperature not specified in the publication
12.3
N1-acetylspermine
37°C, pH 6.5
17
N1-acetylspermine
-
pH 10.0, 30°C, recombinant mutant H64N
44
N1-acetylspermine
37°C, pH 7.5
62
N1-acetylspermine
-
pH 10.0, 30°C, recombinant mutant H64A
78
N1-acetylspermine
pH 9.0, 25°C, recombinant mutant N195A
84
N1-acetylspermine
-
pH 10.0, 30°C, recombinant mutant H64Q
230
N1-acetylspermine
-
pH 10.0, 30°C, recombinant wild-type enzyme
320
N1-acetylspermine
pH 9.0, 25°C, recombinant mutant D94N
1400
N1-acetylspermine
pH 9.0, 25°C, recombinant wild-type Fms1
0.747
norspermine
37°C, pH 6.5
1.64
norspermine
-
pH 6.0, 30°C
2.48
norspermine
-
pH 8.5, 30°C
3.4
norspermine
37°C, pH 7.5
24.4
norspermine
pH 7.5, temperature not specified in the publication
0.08
O2
-
pH 10.0, 30°C, recombinant mutant H64A, with N1-acetylspermine
0.09
O2
-
pH 10.0, 30°C, recombinant mutant H64Q, with N1-acetylspermine
0.11
O2
-
pH 10.0, 30°C, recombinant mutant H64N, with N1-acetylspermine
0.4
O2
-
pH 10.0, 30°C, recombinant mutant H64N, with spermine
0.7
O2
-
pH 10.0, 30°C, recombinant mutant H64Q, with spermine
1
O2
-
pH 10.0, 30°C, recombinant mutants H64A and H64N, with spermine
1
O2
-
pH 8.6, 30°C, recombinant mutant H64A, with N,N'-dibenzyl-1,4-diaminobutane
1.1
O2
-
pH 8.6, 30°C, recombinant mutant H64N, with N,N'-dibenzyl-1,4-diaminobutane
1.3
O2
-
pH 10.0, 30°C, recombinant wild-type enzyme, with N1-acetylspermine
1.4
O2
-
pH 8.6, 30°C, recombinant mutant H64Q, with N,N'-dibenzyl-1,4-diaminobutane
5.5
O2
-
pH 8.6, 30°C, recombinant wild-type enzyme, with N,N'-dibenzyl-1,4-diaminobutane
66
O2
-
pH 10.0, 30°C, recombinant wild-type enzyme, with spermine
100
O2
pH 9.0, 25°C, recombinant mutant D94N, with N1-acetylspermine
104
O2
pH 9.0, 25°C, recombinant mutant D94N, with spermine
327
O2
pH 9.0, 25°C, recombinant mutant N195A, with spermine
358
O2
pH 9.0, 25°C, recombinant wild-type Fms1, with N1-acetylspermine
405
O2
pH 9.0, 25°C, recombinant mutant N195A, with N1-acetylspermine
428
O2
pH 9.0, 25°C, recombinant wild-type Fms1, with spermine
0.185
spermidine
37°C, pH 7.5
0.37
spermidine
pH 8.5, 30°C
11.2
spermidine
pH 7.5, temperature not specified in the publication
12.4
spermidine
pH 7.5, temperature not specified in the publication
0.115
spermine
37°C, pH 6.5
1.4
spermine
-
pH 10.0, 30°C, recombinant mutant H64A
1.6
spermine
-
pH 10.0, 30°C, recombinant mutant H64N
2.7
spermine
37°C, pH 7.5
2.9
spermine
pH 7.5, temperature not specified in the publication
3
spermine
-
pH 10.0, 30°C, recombinant mutant H64Q
3.16
spermine
pH 8.5, 30°C
4.1
spermine
pH 9.35, 25°C, recombinant mutant D94N
5.1
spermine
-
pH 6.0, 30°C
6.4
spermine
-
pH 8.5, 30°C
15.6
spermine
pH 7.5, temperature not specified in the publication
29
spermine
-
pH 10.0, 30°C, recombinant wild-type enzyme
38.5
spermine
pH 9.35, 25°C, recombinant mutant N195A
330
spermine
pH 9.35, 25°C, recombinant wild-type Fms1
400
spermine
-
pH 7.4, 25°C
2.6
thermospermine
37°C, pH 6.5
10
thermospermine
pH 7.5, temperature not specified in the publication
13.8
thermospermine
-
pH 6.0, 30°C
23.3
thermospermine
37°C, pH 7.5
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-
from Pneumocystis carinii infected rats
brenda
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
brenda
-
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
of seedling
brenda
-
brenda
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
brenda
-
-
brenda
-
brenda
greening
brenda
PAO3 promoter activity is detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower
brenda
-
brenda
expression is constitutive, but highest in flower organ
brenda
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
brenda
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
brenda
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
brenda
-
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
-
brenda
-
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
-
brenda
-
brenda
already in very young, completely closed flower buds
brenda
-
brenda
-
-
-
brenda
-
brenda
mostly expressed in the leaves
brenda
most expression of AtPAO3
brenda
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
brenda
PAO3 promoter activity is detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower
brenda
-
brenda
Bjpao1 is predominantly expressed in the notochord, testis and ovary
brenda
-
brenda
Bjpao1 is predominantly expressed in the notochord, testis and ovary
brenda
-
brenda
-
-
-
brenda
-
brenda
in mature pollen grains during pollination and pollen tube growth
brenda
-
-
-
brenda
-
in mature pollen grains during pollination and pollen tube growth
-
brenda
-
brenda
-
brenda
low expression of AtPAO3
brenda
PAO3 promoter activity is detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower
brenda
-
-
-
brenda
-
of seedlings
brenda
-
of seedlings
-
brenda
-
brenda
-
-
-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
brenda
-
root of seedlings
brenda
-
root of seedlings
-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
-
-
-
brenda
-
brenda
Bjpao1 is predominantly expressed in the notochord, testis and ovary
brenda
additional information
isozyme AtPAO3 is abundantly expressed in all tissues
brenda
additional information
-
isozyme AtPAO3 is abundantly expressed in all tissues
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
additional information
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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
brenda
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
brenda
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
brenda
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
brenda
additional information
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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
brenda
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
brenda
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
brenda
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
brenda
additional information
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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
brenda
additional information
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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
-
brenda
additional information
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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
-
brenda
additional information
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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
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brenda
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evolution
AtPAO2-AtPAO4 form a subfamily of polyamine oxxidases different from AtPAO1, EC 1.5.3.16, overview
evolution
Plantae
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identification of four polyamine oxidase subfamilies in plants. Subfamily PAO back conversion 1 (PAObc1) is present on every lineage included in these analyses. Subfamily PAObc2 is exclusively present in vascular plants. The only terminal catabolism (TC) PAO subfamily was lost in Superasterids but it is present in all other land plants. Subfamily PAObc3 is the result of a gene duplication event preceding Angiosperm diversification, followed by a gene extinction in Monocots. Differential conserved protein motifs exist for each subfamily of plant PAOs
evolution
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AtPAO2-AtPAO4 form a subfamily of polyamine oxxidases different from AtPAO1, EC 1.5.3.16, overview
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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
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
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
metabolism
residues Gln94, Tyr403 and Thr440 are predicted to be important in the active site
metabolism
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the enzyme is involved in the polyamine back-conversion pathway, overview
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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
flavoprotein Fms1 catalyzes the oxidation of spermine in the biosynthetic pathway for pantothenic acid
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
stress response
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
physiological function
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the enzyme functions as thermospermine oxidase. The enzyme OsPAO1 from Oryzae sativa is the functional ortholog of enzyme AtPAO5 from Arabidopsis thaliana. OsPAO1 is able to complement the growth defects of Atpao5 deletion mutants
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
physiological function
when PAO5 is expressed in an Arabidopsis thaliana Pao5 mutant, thermospermine level decreases to almost normal values of wild type plants, and norspermidine is produced. The reduced growth phenotype of the mutant strain is cured by the expression of PAO5
physiological function
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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
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additional information
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His64 hydrogen bonds to the reactive nitrogen in the polyamine substrate
additional information
the active site of Fms1 contains three amino acid residues positioned to interact with the polyamine substrate, His67, Asn195, and Asp94. These three residues form a hydrogen-bonding triad with Asn195 being the central residue. His67 is important both for interacting with the substrate and for maintaining the hydrogen bonds in the triad
additional information
the overall catalytic reactions of flavoprotein oxidases such as Fms1 can be divided into reductive and oxidative half-reactions. In the reductive half-reaction, binding of the oxidized substrate is followed by transfer of a hydride equivalent to the flavin to form reduced flavin and oxidized substrate. In the oxidative half-reaction, the reduced flavin is oxidized by molecular oxygen to form H2O2, the oxidized amine then dissociates from the enzyme. A moiety with a pKa value of 7.2-8.3 must be unprotonated for amine oxidation
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