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Information on EC 1.5.3.17 - non-specific polyamine oxidase
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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 expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
+
=
+
+
+
+
=
+
+
Synonyms
atpao5, atpao2, atpao3, ospao1, atpao4, selpao5, polyamine oxidase 1, bjpao2, bjpao1, slr5093, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtPAO2
AtPAO3
AtPAO4
EC 1.5.3.11
-
-
formerly, part transferred
-
Fms1
OsPAO1
PAO
PAO2
PAO3
PAO5
polyamine oxidase 1
T-Spm oxidase
thermospermine oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2
-
-
-
-
N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2
-
-
-
-
spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2
-
-
-
-
spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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).
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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
(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
-
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + 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 + 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
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
?
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
?
-
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
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
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
-
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
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
?
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
?
-
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
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 + ?
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 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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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
spermidine + O2 + H2O
putrescine + 3-aminopropanal + H2O2
-
-
-
?
thermospermine + O2 + H2O
norspermidine + 3-acetamidopropanal + H2O2
norspermidine is generated via thermospermine catabolism in Selaginella lepidophylla
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + 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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
?
-
flavoprotein oxidase Fms1 catalyzes the oxidation of spermine and N1-acetylspermine to spermidine and 3-aminopropanal or N-acetyl-3-aminopropanal
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
purified enzyme shows absorbance peaks at 380 and 450 nm
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithioerythritol
-
up to 0.010 mM increase the enzyme activity, higher concentrations inhibit
dithiothreitol
-
up to 0.010 mM increase the enzyme activity, higher concentrations inhibit
MDL 72145