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Information on EC 1.5.3.16 - spermine oxidase
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1.5.3.16 spermine oxidaseIUBMB Comments
The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency . The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from 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 1.5.3.17 (non-specific polyamine oxidase).
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Word Map
- 1.5.3.16
- polyamine
- putrescine
-
acetylpolyamine
-
back-conversion
- n1-acetylspermine
-
n1-acetylpolyamine
- 3-aminopropanal
- acrolein
-
benspm
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
spermine oxidase, smo(paoh1), atpao1, paoh1/smo, smo/paoh1, msmoalpha, msmomu, ghpao, fms1 protein, spm oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtPAO1
EC 1.5.3.11
-
-
formerly, part transferred
-
mSMO
mSMOmu
PAO4
SMO
SMOX
spermine oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
spermidine:oxygen oxidoreductase (spermidine-forming)
The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency [3]. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from 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 1.5.3.17 (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
1,16-diamino-4,8,13-triazahexadecane + O2 + H2O
?
-
increased activity compared to spermine
-
-
?
N,N'-bis-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
N-(3-aminopropyl)-N'-(3-benzylaminopropyl)butane-1,4-diamine + N1-(3-benzylaminopropyl)butane-1,4-diamine + H2O2 + ?
-
-
main products
-
?
N,N'-bis-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-ethylaminopropyl)butane-1,4-diamine + H2O2 + ?
-
minor N4-endo cleavage pathways resulting in formation of EtDAP
-
-
?
N-(3-aminopropyl)-N-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
spermine + H2O2 + ?
-
-
i.e. N,N'-bis-(3-aminopropyl)butane-1,4-diamine
-
?
N-(3-benzylaminopropyl)-N'-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-ethylaminopropyl)butane-1,4-diamine + H2O2 + ?
-
-
-
-
?
N1-(3-[[(thiophen-2-yl)methyl]amino]propyl)octane-1,8-diamine + O2 + H2O
octane-1,8-diamine + N1-[(thiophen-2-yl)methyl]propanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermine + O2 + H2O
N1-acetylspermidine + 3-aminopropanal + H2O2
-
-
-
-
?
N1-benzyldodecane-1,12-diamine + O2 + H2O
dodecane-1,12-diamine + N1-benzylpropanal + H2O2
-
-
-
?
N1-benzylspermine + O2 + H2O
spermidine + 3-(benzylamino)propanal + H2O2
-
-
-
?
N1-ethyl-spermine + O2 + H2O
spermidine + N-ethyl-3-aminopropanal + H2O2
-
good substrate
-
-
?
N1-monoethylspermine + O2 + H2O
spermidine + ?
98% of the activity with spermine
-
-
?
N1-[(naphthalen-2-yl)methyl]spermine + O2 + H2O
spermidine + N1-[(naphthalen-2-yl)methyl]propanal + H2O2
-
-
-
?
N1-[(pyridin-2-yl)methyl]spermine + O2 + H2O
spermidine + N1-[(pyridin-2-yl)methyl]propanal + H2O2
-
-
-
?
N1-[(thiophen-2-yl)methyl]spermine + O2 + H2O
spermidine + N1-[(thiophen-2-yl)methyl]propanal + 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
?
less than 10% of the activity with spermine, SMO/PAOh1
-
-
?
N1-acetylspermine + O2 + H2O
?
less than 10% of the activity with spermine, splice variant SMO5
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
the ethyl substituent that retains the amine as positively charged, strongly accelerates the reaction velocity
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
mutation E216L/S218A endows the enzyme with N1-acetylspermine oxidase activity
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
less than 10% of the activity with norspermine
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
low activity
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
low activity
-
-
?
norspermine + O2 + H2O
?
the enzyme AtPAO5 has a better activity as a dehydrogenase rather than as an oxidase. With the best electron acceptor (ferricenium), the best in vitro substrate for recombinant AtPAO5 is N1-acetylspermine
-
-
?
spermine + O2 + H2O
?
exhibits a strong preference for spermine as the primary substrate over all other naturally occurring polyamines, SMO/PAOh1
-
-
?
spermine + O2 + H2O
?
exhibits a strong preference for spermine as the primary substrate over all other naturally occurring polyamines, splice variant SMO5
-
-
?
spermine + O2 + H2O
?
mutant mSMOmuDELTA (with a deletion of the nuclear domain A) is not active on spermidine, N1-acetylspermidine or N1-acetylspermine
-
-
?
spermine + O2 + H2O
?
purified isoform mSMOmu oxidizes specifically spermine and is not active on spermidine, N1-acetylspermidine and N1-acetylspermine
-
-
?
spermine + O2 + H2O
?
the mMSO catalytic mechanism is consistent with a simple four-step kinetic scheme. The enzyme is unable to oxidize other free or acetylated polyamines
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
enzyme is involved in a polyamine back-conversion pathway
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
AtPAO4 specifically catalyzes the conversion of spermine to spermidine under the assay conditions
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
at pH 6.5, substrate preference is in the following decreasing order: thermospermine, N1-acetylspermine, norspermine, spermine, spermidine. Spermidine is catabolized at a very low rate. At pH 7.5, substratr preference is in the following decreasing order: spermine, norspermine, N1-acetylspermine, thermospermine, spermidine. Spermidine is catalyzed at a very low rate
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme AtPAO5 has a better activity as a dehydrogenase rather than as an oxidase. With the best electron acceptor (ferricenium), the best in vitro substrate for recombinant AtPAO5 is N1-acetylspermine
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
the enzyme contributes to resistance of the plant against Verticillium dahliae through the mediation of spermine and camalexin signalling
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
preferred substrate
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
SMO may contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-aminopropanal
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
the enzyme specifically oxidizes spermine
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is a regulator of macrophage host response to Helicobacter pylori. It enhances antimicrobial nitric oxide generation by depletion of spermine
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is involved in polyamine catabolism. Highly inducible enzyme that catalyzes the oxidative cleavage of spermine to form spermidine, 3-aminopropanal, and hydrogen peroxide
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
strongly favours spermine over N1-acetylspermine, fails to act on N1-acetylspermidine, spermidine or the preferred PAO substrate, N1,N12-diacetylspermine
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
the enzyme specifically oxidizes spermine
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
SMO oxidizes the carbon on the exo side of the N5-nitrogen of SPM producing spermidine, 3-aminopropanal, and H2O2
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is highly specific for spermine as substrate
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is a regulator of macrophage host response to Helicobacter pylori. It enhances antimicrobial nitric oxide generation by depletion of spermine
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is involved in cell drug response, apoptosis, and in the etiology of several pathologies, including cancer. The Total-Smox line is a genetic model useful to deepen the knowledge on the role of spermine oxidase in muscle atrophy and muscular pathological conditions like dystrophy
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is involved in the catabolism of polyamines
-
-
?
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 + aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
about 20% of the activity with norspermine
-
-
?
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
bets substrate
-
-
?
thermospermine + O2 + H2O
?
the enzyme AtPAO5 has a better activity as a dehydrogenase rather than as an oxidase. With the best electron acceptor (ferricenium), the best in vitro substrate for recombinant AtPAO5 is N1-acetylspermine
-
-
?
thermospermine + O2 + H2O
? + H2O2
about 10% of the activity with spermine
-
-
?
thermospermine + O2 + H2O
? + H2O2
about 65% of the activity with norspermine
-
-
?
additional information
?
-
-
no oxidation activity with spermidine
-
-
?
additional information
?
-
-
no oxidation activity with spermidine
-
-
?
additional information
?
-
AtPAO4 deficiency induces alterations in the expression of genes related to the drought stress response and flavonoid biosynthesis
-
-
?
additional information
?
-
no activity with putrescine, spermidine, N1-acetylspermine
-
-
?
additional information
?
-
peroxisomal polyamine oxidase AtPAO4 is involved in the catabolism of polyamines in leaves, overview
-
-
?
additional information
?
-
no substrate: spermidine, N1-acetylspermine, norspermine
-
-
?
additional information
?
-
no substrate: spermidine, N1-acetylspermine, norspermine
-
-
?
additional information
?
-
-
no substrate: spermidine, N1-acetylspermine, norspermine
-
-
?
additional information
?
-
no substrate: spermidine. Comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
no substrate: spermidine. Comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
-
no substrate: spermidine. Comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
spermidine is oxidized with very low efficiency. Comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
spermidine is oxidized with very low efficiency. Comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
-
spermidine is oxidized with very low efficiency. Comparative study of the catalytic properties of recombinant AtPAO1, AtPAO2, AtPAO3, and AtPAO4. All four enzymes strongly resemble their mammalian counterparts, being able to oxidize the common polyamines Spd and/or Spm through a polyamine backconversion pathway
-
-
?
additional information
?
-
-
N-acetylated polyamines and diamines, e.g. Nl-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
?
-
PAOh1 is upregulated in response to polyamine analogue exposure. N1,N11-bis(ethyl)norspermine results in 5fold induction of PAO mRNA and a more than 3-fold induction of PAO activity
-
-
?
additional information
?
-
-
the major level of control of SMO(PAOh1) expression in response to polyamine analogues exposure is at the level of mRNA
-
-
?
additional information
?
-
-
TNF-alpha exposure leads to the induction of SMO/PAOh1, which produces sufficient H2O2 to result in potentially mutagenic DNA damage and presents a molecular mechanism by which general inflammation can contribute directly to the development of cancer
-
-
?
additional information
?
-
-
no activity with N1-acetylspermine, spermidine, alpha-methylspermidine. No production of spermidine from bis-alpha-methylspermine, hSMO
-
-
?
additional information
?
-
no activity with spermidine. No oxidation of N1,N11-bis(ethyl)norspemine, N1-ethyl-N11-(cyclopropyl)methyl-4,8,diazaundecane, N1-ethyl-N11-(cycloheptyl)methyl-4,8,diazaundecane, (S)-N1-(2-methyl-1-butyl)-N11-ethyl-4,8,diazaundecane, SL-11144, SL-11150, SL-11156 and SL-11093
-
-
?
additional information
?
-
-
no activity with spermidine. No oxidation of N1,N11-bis(ethyl)norspemine, N1-ethyl-N11-(cyclopropyl)methyl-4,8,diazaundecane, N1-ethyl-N11-(cycloheptyl)methyl-4,8,diazaundecane, (S)-N1-(2-methyl-1-butyl)-N11-ethyl-4,8,diazaundecane, SL-11144, SL-11150, SL-11156 and SL-11093
-
-
?
additional information
?
-
no activity with: spermidine, N1,N12-diacetylspermine, N1,N12-diethylspermine, N1,N14-diethylhomospermine, MDL-72527, N1,N11-diethylnorspermine
-
-
?
additional information
?
-
-
no activity with: spermidine, N1,N12-diacetylspermine, N1,N12-diethylspermine, N1,N14-diethylhomospermine, MDL-72527, N1,N11-diethylnorspermine
-
-
?
additional information
?
-
-
SMO/PAOh1 exhibits no oxidase activity when using N1,N12-diacetylspermine, N1-acetylspermidine, N8-acetylspermidine, spermidine, or the polyamine analogues, bis(ethyl)norspermine or N1-ethyl-N11-(cyclopropyl)methyl-4,8,diazaundecane
-
-
?
additional information
?
-
SMO/PAOh1 exhibits no oxidase activity when using N1,N12-diacetylspermine, N1-acetylspermidine, N8-acetylspermidine, spermidine, or the polyamine analogues, bis(ethyl)norspermine or N1-ethyl-N11-(cyclopropyl)methyl-4,8,diazaundecane
-
-
?
additional information
?
-
-
splice variant SMO5 exhibits no oxidase activity when using N1,N12-diacetylspermine, N1-acetylspermidine, N8-acetylspermidine, spermidine, or the polyamine analogues, bis(ethyl)norspermine or N1-ethyl-N11-(cyclopropyl)methyl-4,8,diazaundecane
-
-
?
additional information
?
-
splice variant SMO5 exhibits no oxidase activity when using N1,N12-diacetylspermine, N1-acetylspermidine, N8-acetylspermidine, spermidine, or the polyamine analogues, bis(ethyl)norspermine or N1-ethyl-N11-(cyclopropyl)methyl-4,8,diazaundecane
-
-
?
additional information
?
-
-
assay method development and validation, evaluation of quantitative determination of reaction products, overview
-
-
?
additional information
?
-
-
significant activity of this enzyme also on other linear tetramines (i.e. homospermine and N-butylated spermine) and, more importantly, on linear pentamines
-
-
?
additional information
?
-
-
SMO is capable of metabolizing several N-alkylated polyamine derivatives, substrate specificity, overview. N1-(3-Ethylaminopropyl)butane-1,4-diamine trihydrochloride is a poor substrate
-
-
?
additional information
?
-
-
substrate activities of human spermine oxidase with various linear polyamines, overview. N1-acetyl-spermine is a poor substrate. H2O2 is measured by a HPLC method that analyzed fluorescent dimers derived from the oxidation of homovanillic acid in the presence of horseradish peroxidase
-
-
?
additional information
?
-
in mammalian cells, polyamine catabolism seems to be mediated by the activity of two enzymes, PAO and SMO
-
-
?
additional information
?
-
-
in mammalian cells, polyamine catabolism seems to be mediated by the activity of two enzymes, PAO and SMO
-
-
?
additional information
?
-
spermine oxidase activity is a direct oxidative stress inducer of DNA damage, thus rendering cells more sensitive to radiation and apoptosis
-
-
?
additional information
?
-
-
spermine oxidase activity is a direct oxidative stress inducer of DNA damage, thus rendering cells more sensitive to radiation and apoptosis
-
-
?
additional information
?
-
-
spermine oxidase overactivity can deliver sublethal chronic DNA damage and repair without affecting transcriptional and enzymatic levels of the PA key regulatory enzymes ornithine decarboxylase and spermidine/spermine N1-acetyltransferase
-
-
?
additional information
?
-
fails to act upon spermidine, N1-acetylpolyamines, putrescine and N1-acetylcadaverine
-
-
?
additional information
?
-
-
fails to act upon spermidine, N1-acetylpolyamines, putrescine and N1-acetylcadaverine
-
-
?
additional information
?
-
no activity with spermidine and putrescine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
spermidine + 3-aminopropanal + H2O2
-
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
enzyme is involved in a polyamine back-conversion pathway
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
the enzyme contributes to resistance of the plant against Verticillium dahliae through the mediation of spermine and camalexin signalling
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
SMO may contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-aminopropanal
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
the enzyme specifically oxidizes spermine
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is a regulator of macrophage host response to Helicobacter pylori. It enhances antimicrobial nitric oxide generation by depletion of spermine
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spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is involved in polyamine catabolism. Highly inducible enzyme that catalyzes the oxidative cleavage of spermine to form spermidine, 3-aminopropanal, and hydrogen peroxide
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spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
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the enzyme specifically oxidizes spermine
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spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is a regulator of macrophage host response to Helicobacter pylori. It enhances antimicrobial nitric oxide generation by depletion of spermine
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spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is involved in cell drug response, apoptosis, and in the etiology of several pathologies, including cancer. The Total-Smox line is a genetic model useful to deepen the knowledge on the role of spermine oxidase in muscle atrophy and muscular pathological conditions like dystrophy
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spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
the enzyme is involved in the catabolism of polyamines
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additional information
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no oxidation activity with spermidine
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AtPAO4 deficiency induces alterations in the expression of genes related to the drought stress response and flavonoid biosynthesis
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peroxisomal polyamine oxidase AtPAO4 is involved in the catabolism of polyamines in leaves, overview
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PAOh1 is upregulated in response to polyamine analogue exposure. N1,N11-bis(ethyl)norspermine results in 5fold induction of PAO mRNA and a more than 3-fold induction of PAO activity
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the major level of control of SMO(PAOh1) expression in response to polyamine analogues exposure is at the level of mRNA
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TNF-alpha exposure leads to the induction of SMO/PAOh1, which produces sufficient H2O2 to result in potentially mutagenic DNA damage and presents a molecular mechanism by which general inflammation can contribute directly to the development of cancer
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in mammalian cells, polyamine catabolism seems to be mediated by the activity of two enzymes, PAO and SMO
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additional information
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in mammalian cells, polyamine catabolism seems to be mediated by the activity of two enzymes, PAO and SMO
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additional information
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spermine oxidase activity is a direct oxidative stress inducer of DNA damage, thus rendering cells more sensitive to radiation and apoptosis
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additional information
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spermine oxidase activity is a direct oxidative stress inducer of DNA damage, thus rendering cells more sensitive to radiation and apoptosis
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additional information
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spermine oxidase overactivity can deliver sublethal chronic DNA damage and repair without affecting transcriptional and enzymatic levels of the PA key regulatory enzymes ornithine decarboxylase and spermidine/spermine N1-acetyltransferase
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