1.5.3.14: polyamine oxidase (propane-1,3-diamine-forming)
This is an abbreviated version!
For detailed information about polyamine oxidase (propane-1,3-diamine-forming), go to the full flat file.
Word Map on EC 1.5.3.14
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1.5.3.14
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spermine
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oxidases
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back-conversion
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apoplastic
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thermospermine
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putrescine
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tabacum
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fad-dependent
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tunnel
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barley
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mesocotyl
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1,3-diaminopropane
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tetraamines
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aminoaldehyde
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1,8-diaminooctane
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h2o2-producing
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u-shaped
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guazatine
- 1.5.3.14
- spermine
- oxidases
-
back-conversion
- apoplastic
- thermospermine
- putrescine
- tabacum
-
fad-dependent
-
tunnel
- barley
- mesocotyl
- 1,3-diaminopropane
-
tetraamines
- aminoaldehyde
- 1,8-diaminooctane
-
h2o2-producing
-
u-shaped
- guazatine
Reaction
Synonyms
EC 1.5.3.11, flavin-containing polyamine oxidase, maize PAO, maize polyamine oxidase, MPAO, OsPAO7, PAO, ZmPAO
ECTree
1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.5.3.14 - polyamine oxidase (propane-1,3-diamine-forming)
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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
N1-acetylspermidine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
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-
?
norspermidine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
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-
?
norspermine + O2 + H2O
?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
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-
?
spermidine + O2 + H2O
4-aminobutanal + propane-1,3-diamine + H2O2
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
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-
?
spermine + O2 + H2O
1-(3-aminopropyl)-4-aminobutanal + propane-1,3-diamine + H2O2
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-
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?
spermine + O2 + H2O
N-(3-aminopropyl)-4-aminobutanal + 1,3-diaminopropane + H2O2
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
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-
?
spermine + O2 + H2O
propane-1,3-diamine + N-(3-aminopropyl)-4-aminobutanal + H2O2
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-
-
-
?
thermospermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
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-
?
N1-acetylspermine + O2 + H2O
1,3-diaminopropane + H2O2 + ?
at pH 7.0, 37°C, spermine and spermidine are the preferred substrates for OsPAO7, followed by N1-acetylspermine, N1-acetylspermidine, norspermine, thermospermine and norspermidine. At pH 6.5, 30°C, OsPAO7 shows a similar polyamine preference; it favors spermine and spermidine, followed by N1-acetylspermine, norspermine, thermospermine, N1-acetylspermidine and norspermidine
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-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
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-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
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preferred substrate
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-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
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-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
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preferred substrate
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-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
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-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
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best substrate
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-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
enzyme activity is measured spectrophotometrically by following the formation of a pink adduct resulting from the H2O2-dependent oxidation of 4-aminoantipyrine catalyzed by horseradish peroxidase and the subsequent condensation of oxidized 4-aminoantipyrine with 3,5-dichloro-2-hydroxybenzenesulfonic acid
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-
?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
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-
-
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?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
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-
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?
additional information
?
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H2O2 is the co-substrate for the peroxidase-driven reactions during cell-wall maturation and a key signalling molecule in defence mechanisms
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?
additional information
?
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no activity with the diamines putrescine and cadaverine
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?
additional information
?
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no activity with the diamines putrescine and cadaverine
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?
additional information
?
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no activity with: acetylputrescine, acetylcadaverine
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?
additional information
?
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analysis of polymaine content in leaves under different salt conditions, overview
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?
additional information
?
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effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
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?
additional information
?
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effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
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?
additional information
?
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involvement of polyamine oxidase in abscisic acid-induced cytosolic antioxidant defense in leaves of maize. MPAO contributes to abscisic acid-induced cytosolic antioxidant defense through H2O2, a spermidine catabolic product, overview
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?
additional information
?
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the enzyme from Zea mays oxidizes the carbon on the endo-side of the N5-nitrogen of spermidine and spermine
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?
