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Information on EC 1.5.3.14 - polyamine oxidase (propane-1,3-diamine-forming)
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1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)IUBMB Comments
As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines . This enzyme less efficiently catalyses the oxidation of N1-acetylspermine and spermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
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Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
zmpao, ospao7, maize polyamine oxidase, maize pao, flavin-containing polyamine oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.5.3.11
-
-
formerly, part transferred
-
flavin-containing polyamine oxidase
MPAO
PAO
ZmPAO
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
spermidine + O2 + H2O = propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)
As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines [1]. This enzyme less efficiently catalyses the oxidation of N1-acetylspermine and spermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine 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
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
spermine + O2 + H2O
1-(3-aminopropyl)-4-aminobutanal + propane-1,3-diamine + H2O2
-
-
-
?
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
-
-
?
spermine + O2 + H2O
propane-1,3-diamine + N-(3-aminopropyl)-4-aminobutanal + H2O2
-
-
-
-
?
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
-
-
?
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
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
preferred substrate
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
preferred substrate
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
best substrate
-
-
?
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
-
-
?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
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-
-
-
?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
-
-
-
-
?
additional information
?
-
-
H2O2 is the co-substrate for the peroxidase-driven reactions during cell-wall maturation and a key signalling molecule in defence mechanisms
-
-
?
additional information
?
-
no activity with the diamines putrescine and cadaverine
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-
?
additional information
?
-
-
no activity with the diamines putrescine and cadaverine
-
-
?
additional information
?
-
no activity with: acetylputrescine, acetylcadaverine
-
-
?
additional information
?
-
-
analysis of polymaine content in leaves under different salt conditions, overview
-
-
?
additional information
?
-
-
effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
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-
?
additional information
?
-
effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
-
-
?
additional information
?
-
-
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
?
-
-
the enzyme from Zea mays oxidizes the carbon on the endo-side of the N5-nitrogen of spermidine and spermine
-
-
?
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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
spermine + O2 + H2O
propane-1,3-diamine + N-(3-aminopropyl)-4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
1,3-diaminopropane + 4-aminobutanal + H2O2
-
-
-
-
?
spermidine + O2 + H2O
propane-1,3-diamine + 4-aminobutanal + H2O2
-
-
-
-
?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
-
-
-
-
?
spermine + O2 + H2O
1,3-diaminopropane + 1-(3-aminopropylidene)pyrrolidin-1-ium + H2O2
-
-
-
-
?
additional information
?
-
-
H2O2 is the co-substrate for the peroxidase-driven reactions during cell-wall maturation and a key signalling molecule in defence mechanisms
-
-
?
additional information
?
-
-
analysis of polymaine content in leaves under different salt conditions, overview
-
-
?
additional information
?
-
-
effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
-
-
?
additional information
?
-
effects of increased H2O2 production on the expression of enzymes involved in the antioxidant machinery, overview
-
-
?
additional information
?
-
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
oxidized FAD is the prominent form during steady-state turnover, consistent with the reductive half-reaction being rate-limiting
FAD
the FAD prosthetic group is non-covalently bound to the protein and is deeply embedded within the structure. All FAD atoms are solvent-inaccessible, with the exception of the flavin C5a, N5 and C4a atoms that line the active centre
FAD
-
dependent on. Residue K300 is hydrogen-bound to the N5 atom of FAD via a H2O molecule (HOH309), the only solvent molecule present inside the catalytic site in the enzyme inhibitor complexes. In turn, K300 is the only active-site residue whose conformation changes upon FAD reduction, possibly allowing for a reorientation of the HOH309 molecule. The water molecule might thus function as a hydrogen-bond acceptor with the protonated N5 atom of reduced FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(N1-5-aminopentyl)-N3-(cyclohexylethyl)-N1,N2,N3-tris(tert-butoxycarbonyl)guanidine
-
1,19-bis(ethylamino)-5,10,15-triazanonadecane
-
i.,e. SL-11061, 68% inhibition at 0.5 mM
1-(4-aminobutyl)-3-but-3-en-1-ylguanidine
competitive inhibition of spermidine oxidation
1-(4-aminobutyl)-3-but-3-yn-1-ylguanidine
competitive inhibition of spermidine oxidation
1-(5-aminopentyl)-3-(4-methylpent-3-en-1-yl)guanidine
competitive inhibition of spermidine oxidation
1-(6-aminohexyl)-3-(4-methylpent-3-en-1-yl)guanidine
competitive inhibition of spermidine oxidation
1-(guanidino)-17-(N1-(gamma,gamma-dimethylallyl)guanidino)-9-azaheptadecane tris(trifluoroacetate)
-
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(2-cyclopropylethyl)guanidine
-
1-[7-[(9-carbamimidamidononyl)amino]heptyl]-3-(3-methylbut-3-en-1-yl)guanidine
-
3-(4-methylpent-3-en-1-yl)-1-[9-([7-[(4-methylpent-3-en-1-yl)carbamimidamido]heptyl]amino)nonyl]guanidine
-
3-[(2E)-but-2-en-1-yl]-1-[7-[(9-carbamimidamidononyl)amino]heptyl]guanidine
-
N-prenylagmatine
-
i.e. G3, a specific and selective ZmPAO inhibitor. G3 strongly inhibits lignin and suberin polyphenolic domain deposition along the wound periderm in maize mesocoty
N1,N2-bis(tert-butoxycarbonyl)-N1-(gamma,gamma-dimethylallyl)-S-methylisothiourea
-
N1,N2-bis(tert-butoxycarbonyl)-N1-(gamma,gamma-methylallyl)-S-methylisothiourea
-
N1-(3-methoxybenzyl)-N3-(5-aminopentyl)-N2,N3,N4-tris(tertbutoxycarbonyl)guanidine
-
N1-benzylamine-N3-(gamma,gamma-dimethyallyl)-N2,N3,N4-tris(tert-butoxycarbonyl)guanidine
-
N1-benzylamine-N3-(gamma,gamma-dimethylallyl)guanidine bis-(trifluoroacetate)
-
N1-[(30-aminopropyl)-3-aminopropyl]-N3-(gamma,gamma-dimethylallyl)-N2,N3-bis(tert-butoxycarbonyl)guanidine
-
tert-butyl (2E)-but-2-en-1-yl[(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl]carbamate
-
tert-butyl (4-[(tert-butoxycarbonyl)[(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl]amino]butyl)methylcarbamate
-
tert-butyl (6-aminohexyl)[(tert-butoxycarbonyl)(cyclopropylmethyl)carbamimidoyl]carbamate
-
tert-butyl (6-aminohexyl)[(tert-butoxycarbonyl)[(3E)-4-phenylbut-3-en-1-yl]carbamimidoyl]carbamate
-
tert-butyl benzyl[(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl]carbamate
-
tert-butyl [(1E)-[(tert-butoxycarbonyl)(cyclopropylmethyl)amino](methylsulfanyl)methylidene]carbamate
-
tert-butyl [(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl]prop-2-yn-1-ylcarbamate
-
tert-butyl [(E)-[(tert-butoxycarbonyl)imino](methylsulfanyl)methyl][(2E)-3-phenylprop-2-en-1-yl]carbamate
-
1-(4-aminobutyl)-3-(4-fluorobenzyl)guanidine
competitive inhibition of spermidine oxidation
N,N'''-butane-1,4-diylbis[3-(3-methylbut-2-en-1-yl)guanidine]
competitive inhibition of spermidine oxidation
additional information
docking simulations carried out with the charged and uncharged forms of MPAO inhibitors indicate that the stereoelectronic properties of the MPAO active site are consistent with the binding of inhibitors in the protonated form, a feature which can shed light on the still obscure MPAO catalytic mechanism
-
additional information
-
docking simulations carried out with the charged and uncharged forms of MPAO inhibitors indicate that the stereoelectronic properties of the MPAO active site are consistent with the binding of inhibitors in the protonated form, a feature which can shed light on the still obscure MPAO catalytic mechanism
-
additional information
-
no inhibition by 1,3-diaminopropane (1 mM) and H2O2 (1 mM)
-
additional information
no inhibition by 1,3-diaminopropane (1 mM) and H2O2 (1 mM)
-
additional information
computational structure-function analysis of inhibitors, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Inducible expression of maize polyamine oxidase in the nucleus of MCF-7 human breast cancer cells confers sensitivity to etoposide.
Carcinoma
Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin.
Carcinoma, Hepatocellular
Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin.
Colonic Neoplasms
Maize polyamine oxidase in the presence of spermine/spermidine induces the apoptosis of LoVo human colon adenocarcinoma cells.
Neoplasms
Inhibition of polyamine oxidase activity affects tumor development during the maize-Ustilago maydis interaction.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.7