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1,16-diamino-4,8,13-triazahexadecane + O2 + H2O
?
-
increased activity compared to spermine
-
-
?
1,16-diamino-4,8,13-triazahexadecane pentahydrochloride + O2 + H2O
?
-
-
-
-
?
alpha-methylspermine + O2 + H2O
?
-
-
-
-
?
benzylamidine + O2 + H2O
?
-
-
-
-
?
N,N'-bis(3-aminopropyl)ethylenediamine + O2 + H2O
?
-
-
-
-
?
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-acetylspermidine + O2 + H2O
putrescine + ?
-
-
-
-
?
N1-acetylspermine + O2 + H2O
?
N1-acetylspermine + O2 + H2O
N1-acetylspermidine + 3-aminopropanal + H2O2
-
-
-
-
?
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
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]dodecane-1,12-diamine + O2 + H2O
?
-
-
-
?
N1-[(thiophen-2-yl)methyl]spermine + O2 + H2O
spermidine + N1-[(thiophen-2-yl)methyl]propanal + H2O2
-
-
-
?
N8-acetylspermidine + O2 + H2O
1,3-diaminopropane + ?
-
-
-
-
?
norspermidine + O2 + H2O
?
-
-
-
-
?
norspermine + O2 + H2O
? + H2O2
spermidine + O2 + H2O
?
-
-
-
-
?
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 + ?
-
-
-
?
tryptamine + O2 + H2O
?
-
-
-
-
?
additional information
?
-
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
?
very poor substrate
-
-
?
N1-acetylspermine + O2 + H2O
?
weak activity
-
-
?
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
-
-
-
-
?
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
?
-
-
-
-
?
norspermine + O2 + H2O
?
-
-
-
?
norspermine + O2 + H2O
?
-
-
-
?
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
? + H2O2
-
-
-
?
norspermine + O2 + H2O
? + H2O2
best substrate
-
-
?
spermine + O2 + H2O
?
-
-
-
-
?
spermine + O2 + H2O
?
-
-
-
?
spermine + O2 + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
-
?
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
-
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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 20% of the activity with norspermine
-
-
?
spermine + O2 + H2O
spermidine + aminopropanal + H2O2
bets substrate
-
-
?
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
? + H2O2
-
-
-
?
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 activity with spermidine
-
-
?
additional information
?
-
no activity with spermidine
-
-
?
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
?
-
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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
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additional information
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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
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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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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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fails to act upon spermidine, N1-acetylpolyamines, putrescine and N1-acetylcadaverine
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fails to act upon spermidine, N1-acetylpolyamines, putrescine and N1-acetylcadaverine
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additional information
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no activity with spermidine and putrescine
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no activity with spermidine and putrescine
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Adenocarcinoma
Induction of the PAOh1/SMO polyamine oxidase by polyamine analogues in human lung carcinoma cells.
Brain Infarction
Aggravation of brain infarction through an increase in acrolein production and a decrease in glutathione with aging.
Brain Injuries
Astrocyte-Dependent Vulnerability to Excitotoxicity in Spermine Oxidase-Overexpressing Mouse.
Breast Neoplasms
Spermine oxidase (SMO) activity in breast tumor tissues and biochemical analysis of the anticancer spermine analogues BENSpm and CPENSpm.
Breast Neoplasms
Spermine oxidase SMO(PAOh1), Not N1-acetylpolyamine oxidase PAO, is the primary source of cytotoxic H2O2 in polyamine analogue-treated human breast cancer cell lines.
Carcinogenesis
Epigenetic silencing of miR-124 prevents spermine oxidase regulation: implications for Helicobacter pylori-induced gastric cancer.
Carcinogenesis
Increased spermine oxidase expression in human prostate cancer and prostatic intraepithelial neoplasia tissues.
Carcinogenesis
Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology.
Carcinogenesis
The Mechanism of Bacteroides fragilis Toxin Contributes to Colon Cancer Formation.
Carcinogenesis
Tumor necrosis factor-alpha increases reactive oxygen species by inducing spermine oxidase in human lung epithelial cells: a potential mechanism for inflammation-induced carcinogenesis.
Carcinoma
Induction of the PAOh1/SMO polyamine oxidase by polyamine analogues in human lung carcinoma cells.
Carcinoma, Hepatocellular
Spermine oxidase is upregulated and promotes tumor growth in hepatocellular carcinoma.
Colitis
Distinct Immunomodulatory Effects of Spermine Oxidase in Colitis Induced by Epithelial Injury or Infection.
Colitis, Ulcerative
Increased expression and cellular localization of spermine oxidase in ulcerative colitis and relationship to disease activity.
Colorectal Neoplasms
Polyamine catabolism in colorectal cancer cells following treatment with oxaliplatin, 5-fluorouracil and N1, N11 diethylnorspermine.
Colorectal Neoplasms
The roles of microbial products in the development of colorectal cancer: a review.
Diabetic Nephropathies
Polyamines in renal failure.
Diabetic Retinopathy
Spermine oxidase: A promising therapeutic target for neurodegeneration in diabetic retinopathy.
Epilepsy
Epileptic seizures and oxidative stress in a mouse model over-expressing spermine oxidase.
Gastritis
Epigenetic silencing of miR-124 prevents spermine oxidase regulation: implications for Helicobacter pylori-induced gastric cancer.
Gastritis
Spermine oxidation induced by Helicobacter pylori results in apoptosis and DNA damage: implications for gastric carcinogenesis.
Glomerulonephritis
Polyamines in renal failure.
Herpes Zoster
Identification of reproduction-related genes and SSR-markers through expressed sequence tags analysis of a monsoon breeding carp rohu, Labeo rohita (Hamilton).
Hypersensitivity
Chronic sub-lethal oxidative stress by spermine oxidase overactivity induces continuous DNA repair and hypersensitivity to radiation exposure.
Infections
Cotton polyamine oxidase is required for spermine and camalexin signalling in the defence response to Verticillium dahliae.
Infections
Distinct Immunomodulatory Effects of Spermine Oxidase in Colitis Induced by Epithelial Injury or Infection.
Infections
Increased Helicobacter pylori-associated gastric cancer risk in the Andean region of Colombia is mediated by spermine oxidase.
Infections
Spermine oxidation induced by Helicobacter pylori results in apoptosis and DNA damage: implications for gastric carcinogenesis.
Inflammatory Bowel Diseases
The roles of microbial products in the development of colorectal cancer: a review.
Kidney Failure, Chronic
Polyamine oxidase and acrolein as novel biochemical markers for diagnosis of cerebral stroke.
Kidney Failure, Chronic
Polyamines in renal failure.
Lung Neoplasms
Induction of the PAOh1/SMO polyamine oxidase by polyamine analogues in human lung carcinoma cells.
Muscular Atrophy
Spermine oxidase maintains basal skeletal muscle gene expression and fiber size and is strongly repressed by conditions that cause skeletal muscle atrophy.
Neoplasms
Genetic regulation of spermine oxidase activity and cancer risk: a Mendelian randomization study.
Neoplasms
Increased spermine oxidase expression in human prostate cancer and prostatic intraepithelial neoplasia tissues.
Neoplasms
Induction of the PAOh1/SMO polyamine oxidase by polyamine analogues in human lung carcinoma cells.
Neoplasms
Inflammation and polyamine catabolism: the good, the bad and the ugly.
Neoplasms
Purvalanol A is a strong apoptotic inducer via activating polyamine catabolic pathway in MCF-7 estrogen receptor positive breast cancer cells.
Neoplasms
Spermine metabolism and radiation-derived reactive oxygen species for future therapeutic implications in cancer: an additive or adaptive response.
Neoplasms
Spermine oxidase is upregulated and promotes tumor growth in hepatocellular carcinoma.
Neoplasms
The polyamine analog PG11047 potentiates the antitumor activity of cisplatin and bevacizumab in preclinical models of lung and prostate cancer.
Neoplasms
The roles of microbial products in the development of colorectal cancer: a review.
Neoplasms
Tumor necrosis factor-alpha increases reactive oxygen species by inducing spermine oxidase in human lung epithelial cells: a potential mechanism for inflammation-induced carcinogenesis.
Nephrosclerosis
Polyamines in renal failure.
Neuroblastoma
Chronic sub-lethal oxidative stress by spermine oxidase overactivity induces continuous DNA repair and hypersensitivity to radiation exposure.
Neuroblastoma
Direct oxidative DNA damage, apoptosis and radio sensitivity by spermine oxidase activities in mouse neuroblastoma cells.
Neuroblastoma
HIV-Tat Induces the Nrf2/ARE Pathway through NMDA Receptor-Elicited Spermine Oxidase Activation in Human Neuroblastoma Cells.
Neuroblastoma
Link between spermine oxidase and apoptosis antagonizing transcription factor: A new pathway in neuroblastoma.
Neuroblastoma
Mouse spermine oxidase gene splice variants. Nuclear subcellular localization of a novel active isoform.
Ovarian Neoplasms
Polyamine catabolism in platinum drug action: Interactions between oxaliplatin and the polyamine analogue N1,N11-diethylnorspermine at the level of spermidine/spermine N1-acetyltransferase.
Pancreatitis
[Methylated analogues of spermine and spermidine as tools to investigate cellular functions of polyamines and the enzymes of their metabolism]
Prostatic Intraepithelial Neoplasia
Increased spermine oxidase expression in human prostate cancer and prostatic intraepithelial neoplasia tissues.
Prostatic Neoplasms
Increased spermine oxidase expression in human prostate cancer and prostatic intraepithelial neoplasia tissues.
Prostatic Neoplasms
Polyamine Analogues of Propanediamine Series Inhibit Prostate Tumor Cell Growth and Activate the Polyamine Catabolic Pathway.
Reperfusion Injury
The Role of Spermidine/Spermine-N1-Acetyltransferase in Endotoxin-Induced Acute Kidney Injury.
Seizures
Astrocyte-Dependent Vulnerability to Excitotoxicity in Spermine Oxidase-Overexpressing Mouse.
Seizures
Epileptic seizures and oxidative stress in a mouse model over-expressing spermine oxidase.
Stomach Diseases
Human and Helicobacter pylori Interactions Determine the Outcome of Gastric Diseases.
Stomach Neoplasms
Epigenetic silencing of miR-124 prevents spermine oxidase regulation: implications for Helicobacter pylori-induced gastric cancer.
Stomach Neoplasms
Increased Helicobacter pylori-associated gastric cancer risk in the Andean region of Colombia is mediated by spermine oxidase.
Stomach Neoplasms
Spermine oxidase mediates Helicobacter pylori-induced gastric inflammation, DNA damage, and carcinogenic signaling.
Stomach Neoplasms
Spermine Oxidase Mediates the Gastric Cancer Risk Associated With Helicobacter pylori CagA.
Stomach Neoplasms
Spermine oxidase, a polyamine catabolic enzyme that links Helicobacter pylori CagA and gastric cancer risk.
Stomach Neoplasms
Spermine oxidation induced by Helicobacter pylori results in apoptosis and DNA damage: implications for gastric carcinogenesis.
Stroke
Acrolein, IL-6 and CRP as markers of silent brain infarction.
Zika Virus Infection
Polymeric Prodrugs Targeting Polyamine Metabolism Inhibit Zika Virus Replication.
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evolution
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AtPAO2-AtPAO4 form a subfamily of polyamine oxidases different from AtPAO1, overview
evolution
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isozyme SMOalpha displays a significant sequence similarity with the structurally characterized polyamine oxidase from maize
evolution
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phylogenetic analysis and structure-function relationships of spermine oxidases among vertebrates, overview. Polar residues (His82, Gln200, Glu224, Tyr482, Ser527, Thr528) and hydrophobic residues (Trp80 and Trp427), hypothesized to bind spermine in the correct position, are strictly conserved in all SMOs
evolution
phylogenetic analysis and structure-function relationships of spermine oxidases among vertebrates, overview. Polar residues (His82, Gln200, Glu224, Tyr482, Ser527, Thr528) and hydrophobic residues (Trp80 and Trp427), hypothesized to bind spermine in the correct position, are strictly conserved in all SMOs
evolution
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phylogenetic analysis and structure-function relationships of spermine oxidases among vertebrates, ubiquitous occurrence of these SMO isoforms in placental mammals, overview. Polar residues (His82, Gln200, Glu224, Tyr482, Ser527, Thr528) and hydrophobic residues (Trp80 and Trp427), hypothesized to bind spermine in the correct position, are strictly conserved in all SMOs
evolution
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AtPAO2-AtPAO4 form a subfamily of polyamine oxidases different from AtPAO1, overview
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malfunction
AtPAO4 deficiency induces alterations in the expression of genes related to the drought stress response and flavonoid biosynthesis
malfunction
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decreased expression of SMO is observed in brains of suicide completers. SMO dysregulation can alter polyamine homeostasis affecting polyamine catabolism, which has been observed to be often associated with several disease states. The late induction of SMO correlates very well with Spm increase in the ipsilateral injured regions compared to equivalent controlateral regions, suggesting that SMO activity might be elevated at later times post-injury. Spermine oxidation may also be considered a source of secondary tissue damage, increased inflammation and apoptotic cell death in the injured brain
malfunction
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SMO dysregulation can alter polyamine homeostasis affecting polyamine catabolism, which has been observed to be often associated with several disease states
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
reduced spermine oxidase expression may contribute to muscle atrophy during a variety of stress conditions, including immobilization, denervation, fasting, and aging
metabolism
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SMO is a key enzyme of polyamine catabolism, metabolism of N-alkylated spermine analogues by polyamine and spermine oxidases, overview
metabolism
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the enzyme is essential for polyamine homeostasis, which is mandatory for cellular life
metabolism
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the enzyme is essential for polyamine homeostasis, which is mandatory for cellular life
metabolism
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the enzyme is involved in polyamine catabolic pathways, overview
metabolism
the enzyme is involved in polyamine catabolism
metabolism
the enzyme is involved in the catabolism of polyamines
physiological function
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involvement of SMO in gastritic mucosal inflammation, SMO expression is increased in human prostate cancer and prostate intraepithelial neoplasia tissues. Polyamines are ubiquitous, polycationic alkylamines that are essential for eukaryotic cell growth and differentiation, and play an important role in inflammation-induced carcinogenesis. Increased expression and cellular localization of spermine oxidase in ulcerative colitis and relationship to disease activity
physiological function
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spermine oxidase plays a role as a mediator of reactive oxygen species production in HIV-Tat-induced neuronal toxicity. HIV-1 Tat protein is found to induce reactive oxygen species production and to affect cell viability in SH-SY5Y cells, these effects being mediated by spermine oxidase. Pretreatment of cells with N-acetylcysteine, a scavenger of H2O2, and with MK-801 is able to completely inhibit reactive oxygen species formation and to restore cell viability, overview
physiological function
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the oxidative products of SMO activity are spermidine, and the reactive oxygen species H2O2 and the aldehyde 3-aminopropanal each with the potential to produce cellular damages and pathologies. The SMO substrate Spm is a tetramine that plays mandatory roles in several cell functions, such as DNA synthesis, cellular proliferation, modulation of ion channels function, cellular signaling, nitric oxide synthesis and inhibition of immune responses. The enzyme participates in drug response, apoptosis, etiology of several pathological conditions, including cancer, SMO expression appears to be regulated predominantly at the transcriptional level and by messenger RNA stabilization. SMO substrate spermine has an important role in brain functions, since intracellular spermine is responsible for intrinsic gating and rectification of strong inward rectifier K+ channels by directly plugging the ion channel pore. That way, intracellular spermine can also cause inward rectification at some subtypes of alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid and kainate Ca2+-permeable receptors in the central nervous system
physiological function
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the oxidative products of SMO activity are spermidine, and the reactive oxygen species H2O2 and the aldehyde 3-aminopropanal each with the potential to produce cellular damages and pathologies. The SMO substrate Spm is a tetramine that plays mandatory roles in several cell functions, such as DNA synthesis, cellular proliferation, modulation of ion channels function, cellular signaling, nitric oxide synthesis and inhibition of immune responses. The enzyme participates in drug response, apoptosis, etiology of several pathological conditions, including cancer, SMO expression appears to be regulated predominantly at the transcriptional level and by messenger RNA stabilization. SMO substrate spermine has an important role in brain functions, since intracellular spermine is responsible for intrinsic gating and rectification of strong inward rectifier K+ channels by directly plugging the ion channel pore. That way, intracellular spermine can also cause inward rectification at some subtypes of alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid and kainate Ca2+-permeable receptors in the central nervous system
physiological function
senescence
physiological function
spermine oxidase as an important positive regulator of muscle gene expression and fiber size
physiological function
stress response
physiological function
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the enzyme contributes to resistance of the plant against Verticillium dahliae through the mediation of spermine and camalexin signalling
physiological function
the enzyme is a regulator of macrophage host response to Helicobacter pylori. It enhances antimicrobial nitric oxide generation by depletion of spermine
physiological function
the enzyme is a regulator of macrophage host response to Helicobacter pylori. It enhances antimicrobial nitric oxide generation by depletion of spermine
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 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 muscularpathological conditions like dystrophy
physiological function
the enzyme regulates thermospermine homeostasis through a thermospermine oxidation pathway
physiological function
spermine oxidase, as a hydrogen peroxide producer, may be involved in the oxidative stress during epilepsy. In a mouse model overexpressing SMOX specifically in the brain cortex, transgenic mice compared to controls showed a higher susceptibility towards pentylentetrazole and display an altered polyamine content with rise of 8-oxo-7,8-dihydro-2'-deoxyguanosine level, and an augmentation of system xc- as a defence mechanism
physiological function
during C2-C12 myotube differentiation, linear and circular RNA derived from SMOX gene show the same trend of expression. In atrophy, circSMOX levels significantly increase compared to the physiological state, in both in vitro and in vivo models. In both amyotrophic lateral sclerosis mouse models studied, an increased expression of circSMOX and a decreased expression of the linear SMOX mRNA are observed
physiological function
SMOX plays a role in the formation of bile canalicular lumen in liver cells. Knockdown of SMOX reduces the formation of bile canalicular lumen. Phosphorylated protein kinase B is localized to canalicular lumen and treatment with an inhibitor significantly reduces the formation of bile canalicular lumen. Acrolein scavenger also inhibits the formation of bile canalicular lumen. Tumor suppressor PTEN, phosphatase and tensin homolog and an inhibitor of protein kinase B are alkylated in a SMOX-dependent manner
additional information
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in human SMO1, the active site is characterized by a negatively charged specificity pocket, formed by residues Glu216 and Ser218, which allows binding of Spm, possessing a protonated primary amino group, but negatively selects N1-acetyl-spermine in which the corresponding group is neutral and possesses a hydrophobic methyl group
additional information
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method development for determination of polyamines and acetylpolyamines in the polyamine catabolic pathway creating heptafluorobutyryl derivatives of the compounds for TOF and hybrid tandem mass spectrometry, overview
additional information
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molecular modelling of SMOalpha three-dimensional structure, active site residues are His82 and Tyr482. The substrate is bound in the correct position to undergo oxidation through a series of electrostatic interactions involving the substrate amino groups and the protein residues His82, Gln200, Glu224, Tyr482, and Ser527, overview
additional information
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substrate binding and catalytic mechanism, spermine docking into the active site, CD spectroscopy, structure modelling, overview
additional information
substrate binding and catalytic mechanism, spermine docking into the active site, CD spectroscopy, structure modelling, overview
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Wang, Y.; Devereux, W.; Woster, P.M.; Stewart, T.M.; Hacker, A.; Casero, R.A., Jr.
Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure
Cancer Res.
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2001
Homo sapiens (Q9NWM0)
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Landry, J.; Sternglanz, R.
Yeats Fms1 is a FAD-utilizing polyamine oxidase
Biochem. Biophys. Res. Commun.
303
771-776
2003
Saccharomyces cerevisiae
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Wang, Y.; Murray-Stewart, T.; Devereux, W.; Hacker, A.; Frydman, B.; Woster, P.M.; Casero, R.A.Jr.
Properties of purified human polyamine oxidase, PAOh1/SMO
Biochem. Biophys. Res. Commun.
304
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2003
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Inhibition of polyamine and spermine oxidases by polyamine analogues
FEBS J.
273
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Tavladoraki, P.; Rossi, M.N.; Saccuti, G.; Perez-Amador, M.A.; Polticelli, F.; Angelini, R.; Federico, R.
Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion
Plant Physiol.
141
1519-1532
2006
Arabidopsis thaliana (Q9FNA2)
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Bellelli, A.; Cavallo, S.; Nicolini, L.; Cervelli, M.; Bianchi, M.; Mariottini, P.; Zelli, M.; Federico, R.
Mouse spermine oxidase: a model of the catalytic cycle and its inhibition by N,N1-bis(2,3-butadienyl)-1,4-butanediamine
Biochem. Biophys. Res. Commun.
322
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2004
Mus musculus (Q99K82), Mus musculus
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Müller, S.; Walter, R.D.
Purification and characterization of polyamine oxidase from Ascaris suum
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1992
Ascaris suum
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Vujcic, S.; Diegelman, P.; Bacchi, C.J.; Kramer, D.L.; Porter, C.W.
Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin
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367
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Wang, Y.; Hacker, A.; Murray-Stewart, T.; Fleischer, J.G.; Woster, P.M.
Induction of human spermine oxidase SMO(PAOh1) is regulated at the levels of new mRNA synthesis, mRNA stabilization and newly synthesized protein
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386
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Homo sapiens
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Amendolaa, R.; Bellini, A.; Cervelli, M.; Deganc, P.; Marcoccid, L.; Martinie, F.; Mariottini, P.
Direct oxidative DNA damage, apoptosis and radio sensitivity by spermine oxidase activities in mouse neuroblastoma cells
Biochim. Biophys. Acta
1755
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2005
Mus musculus (Q99K82), Mus musculus
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Bianchi, M.; Bellini, A.; Cervelli, M.; Degan, P.; Narcocci, L.; Martini, F; Scatteia, M.; Mariottini, P.; Amendola, R.
Chronic sub-lethal oxidative stress by spermine oxidase overactivity induces continuous DNA repair and hypersensitivity to radiation exposure
Biochim. Biophys. Acta
1773
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2007
Mus musculus
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Babbar, N.; Casero, R.A.
Tumor necrosis factor-alpha increases reactive oxygen species by inducing spermine oxidase in human lung epithelial cells: a potential mechanism for inflammation-induced carcinogenesis
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66
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2006
Homo sapiens
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Cervelli, M.; Bellini, A.; Bianchi, M.; Marcocci, L.; Nocera, S.; Polticelli, F.; Federico, R.; Amendola, R.; Mariottini, P.
Mouse spermine oxidase gene splice variants. Nuclear subcellular localization of a novel active isoform
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760
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2004
Mus musculus (Q99K82), Mus musculus
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Bianchi, M.; Amendola, R.; Federico, R.; Polticelli, F.; Mariottin, P.
Two short protein domains are responsible for the nuclear localization of the mouse spermine oxidase mu isoform
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Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology
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Cervelli, M.; Fratini, E.; Amendola, A.; Bianchi, M.; Signori, E.; Ferraro, E.; Lisi, A.; Federico, R.; Marcocci, L.; Mariottini, P.
Increased spermine oxidase (SMO) activity as a novel differentiation marker of myogenic C2C12 cells
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41
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Heterologous expression and characterization of mouse spermine oxidase
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278
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Spermine oxidase SMO(PAOh1), not N1-acetylpolyamine oxidase PAO, is the primary source of cytotoxic H2O2 in polyamine analogue-treated human breast cancer cell lines
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280
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Müller, S.; Hunter, K.J.; Walter, R.D.
Effect of haloallylamines on polyamine oxidase activity and spermine levels in Ascaris suum
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Kamada-Nobusada, T.; Hayashi, M.; Fukazawa, M.; Sakakibara, H.; Nishimura, M.
A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine catabolism in Arabidopsis thaliana
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49
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2008
Arabidopsis thaliana (Q8H191)
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Goodwin, A.C.; Jadallah, S.; Toubaji, A.; Lecksell, K.; Hicks, J.L.; Kowalski, J.; Bova, G.S.; de Marzo, A.M.; Netto, G.J.; Casero, R.A.
Increased spermine oxidase expression in human prostate cancer and prostatic intraepithelial neoplasia tissues
Prostate
68
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Homo sapiens
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Tavladoraki, P.; Cervelli, M.; Antonangeli, F.; Minervini, G.; Stano, P.; Federico, R.; Mariottini, P.; Polticelli, F.
Probing mammalian spermine oxidase enzyme-substrate complex through molecular modeling, site-directed mutagenesis and biochemical characterization
Amino Acids
40
1115-1126
2011
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Adachi, M.S.; Juarez, P.R.; Fitzpatrick, P.F.
Mechanistic studies of human spermine oxidase: kinetic mechanism and pH effects
Biochemistry
49
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2010
Homo sapiens
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Cervelli, M.; Bellavia, G.; Fratini, E.; Amendola, R.; Polticelli, F.; Barba, M.; Federico, R.; Signore, F.; Gucciardo, G.; Grillo, R.; Woster, P.; Casero Jr, R.; Mariottini, P.
Spermine oxidase (SMO) activity in breast tumor tissues and biochemical analysis of the anticancer spermine analogues BENSpm and CPENSpm
BMC Cancer
10
555
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Homo sapiens, Mus musculus
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Fiori, L.M.; Turecki, G.
Genetic and epigenetic influences on expression of spermine synthase and spermine oxidase in suicide completers
Int. J. Neuropsychopharmacol.
13
725-736
2010
Homo sapiens
brenda
Stanic, I.; Facchini, A.; Borzi, R.; Stefanelli, C.; Flamigni, F.
The polyamine analogue N1,N11-diethylnorspermine can induce chondrocyte apoptosis independently of its ability to alter metabolism and levels of natural polyamines
J. Cell. Physiol.
219
109-116
2009
Homo sapiens
brenda
Fincato, P.; Moschou, P.N.; Spedaletti, V.; Tavazza, R.; Angelini, R.; Federico, R.; Roubelakis-Angelakis, K.A.; Tavladoraki, P.
Functional diversity inside the Arabidopsis polyamine oxidase gene family
J. Exp. Bot.
6
1155-1168
2010
Arabidopsis thaliana (Q8H191), Arabidopsis thaliana (Q9FNA2), Arabidopsis thaliana
brenda
Takahashi, Y.; Cong, R.; Sagor, G.H.; Niitsu, M.; Berberich, T.; Kusano, T.
Characterization of five polyamine oxidase isoforms in Arabidopsis thaliana
Plant Cell Rep.
29
955-965
2010
Arabidopsis thaliana (Q8H191), Arabidopsis thaliana (Q9FNA2), Arabidopsis thaliana
brenda
Häkkinen, M.; Hyönen, M.; Auriola, S.; Casero Jr., R.; Vepsäläinen, J.; Khomutov, A.; Alhonen, L.; Keinänen, T.
Metabolism of N-alkylated spermine analogues by polyamine and spermine oxidases
Amino Acids
38
369-381
2010
Homo sapiens
brenda
Cervelli, M.; Amendola, R.; Polticelli, F.; Mariottini, P.
Spermine oxidase: ten years after
Amino Acids
42
441-450
2012
Homo sapiens, Mus musculus
brenda
Fincato, P.; Moschou, P.N.; Ahou, A.; Angelini, R.; Roubelakis-Angelakis, K.A.; Federico, R.; Tavladoraki, P.
The members of Arabidopsis thaliana PAO gene family exhibit distinct tissue- and organ-specific expression pattern during seedling growth and flower development
Amino Acids
42
831-841
2012
Arabidopsis thaliana
brenda
Moriya, S.; Iwasaki, K.; Samejima, K.; Takao, K.; Kohda, K.; Hiramatsu, K.; Kawakita, M.
A mass spectrometric method to determine activities of enzymes involved in polyamine catabolism
Anal. Chim. Acta
748
45-52
2012
Homo sapiens
brenda
Takao, K.; Shirahata, A.; Samejima, K.; Casero, R.A.; Igarashi, K.; Sugita, Y.
Pentamines as substrate for human spermine oxidase
Biol. Pharm. Bull.
36
407-411
2013
Homo sapiens
brenda
Capone, C.; Cervelli, M.; Angelucci, E.; Colasanti, M.; Macone, A.; Mariottini, P.; Persichini, T.
A role for spermine oxidase as a mediator of reactive oxygen species production in HIV-Tat-induced neuronal toxicity
Free Radic. Biol. Med.
63
99-107
2013
Homo sapiens
brenda
Hong, S.K.; Chaturvedi, R.; Piazuelo, M.B.; Coburn, L.A.; Williams, C.S.; Delgado, A.G.; Casero, R.A.; Schwartz, D.A.; Wilson, K.T.
Increased expression and cellular localization of spermine oxidase in ulcerative colitis and relationship to disease activity
Inflamm. Bowel Dis.
16
1557-1566
2010
Homo sapiens
brenda
Fincato, P.; Moschou, P.N.; Spedaletti, V.; Tavazza, R.; Angelini, R.; Federico, R.; Roubelakis-Angelakis, K.A.; Tavladoraki, P.
Functional diversity inside the Arabidopsis polyamine oxidase gene family
J. Exp. Bot.
62
1155-1168
2011
Arabidopsis thaliana, Arabidopsis thaliana Columbia-0
brenda
Cervelli, M.; Salvi, D.; Polticelli, F.; Amendola, R.; Mariottini, P.
in the evolutionary framework of spermine oxidase
J. Mol. Evol.
76
365-370
2013
Homo sapiens, vertebrata, Mus musculus (Q99K82)
brenda
Bongers, K.S.; Fox, D.K.; Kunkel, S.D.; Stebounova, L.V.; Murry, D.J.; Pufall, M.A.; Ebert, S.M.; Dyle, M.C.; Bullard, S.A.; Dierdorff, J.M.; Adams, C.M.
Spermine oxidase maintains basal skeletal muscle gene expression and fiber size and is strongly repressed by conditions that cause skeletal muscle atrophy
Am. J. Physiol. Endocrinol. Metab.
308
E144-E158
2015
Mus musculus (Q99K82), Mus musculus
brenda
Chaturvedi, R.; Asim, M.; Barry, D.P.; Frye, J.W.; Casero, R.A.; Wilson, K.T.
Spermine oxidase is a regulator of macrophage host response to Helicobacter pylori enhancement of antimicrobial nitric oxide generation by depletion of spermine
Amino Acids
46
531-542
2014
Mus musculus (Q99K82), Mus musculus, Homo sapiens (Q9NWM0), Homo sapiens
brenda
Cervelli, M.; Leonetti, A.; Cervoni, L.; Ohkubo, S.; Xhani, M.; Stano, P.; Federico, R.; Polticelli, F.; Mariottini, P.; Agostinelli, E.
Stability of spermine oxidase to thermal and chemical denaturation comparison with bovine serum amine oxidase
Amino Acids
48
2283-2291
2016
Mus musculus (Q99K82)
brenda
Cervelli, M.; Angelucci, E.; Stano, P.; Leboffe, L.; Federico, R.; Antonini, G.; Mariottini, P.; Polticelli, F.
The Glu216/Ser218 pocket is a major determinant of spermine oxidase substrate specificity
Biochem. J.
461
453-459
2014
Mus musculus (Q99K82)
brenda
Moriya, S.S.; Miura, T.; Takao, K.; Sugita, Y.; Samejima, K.; Hiramatsu, K.; Kawakita, M.
Development of irreversible inactivators of spermine oxidase and N1-acetylpolyamine oxidase
Biol. Pharm. Bull.
37
475-480
2014
Homo sapiens (Q9NWM0), Homo sapiens
brenda
Sagor, G.H.; Inoue, M.; Kim, D.W.; Kojima, S.; Niitsu, M.; Berberich, T.; Kusano, T.
The polyamine oxidase from lycophyte Selaginella lepidophylla (SelPAO5), unlike that of angiosperms, back-converts thermospermine to norspermidine
FEBS Lett.
589
3071-3078
2015
Selaginella lepidophylla (A0A0M3VGH5)
brenda
Ceci, R.; Duranti, G.; Leonetti, A.; Pietropaoli, S.; Spinozzi, F.; Marcocci, L.; Amendola, R.; Cecconi, F.; Sabatini, S.; Mariottini, P.; Cervelli, M.
Adaptive responses of heart and skeletal muscle to spermine oxidase overexpression Evaluation of a new transgenic mouse model
Free Radic. Biol. Med.
103
216-225
2017
Mus musculus (Q99K82), Mus musculus
brenda
Bonaiuto, E.; Grancara, S.; Martinis, P.; Stringaro, A.; Colone, M.; Agostinelli, E.; Macone, A.; Stevanato, R.; Vianello, F.; Toninello, A.; Di Paolo, M.L.
A novel enzyme with spermine oxidase properties in bovine liver mitochondria identification and kinetic characterization
Free Radic. Biol. Med.
81
88-99
2015
Bos taurus
brenda
Tavladoraki, P.; Cona, A.; Angelini, R.
Copper-containing amine oxidases and FAD-dependent polyamine oxidases are key players in plant tissue differentiation and organ development
Front. Plant Sci.
7
824
2016
Arabidopsis thaliana (Q8H191), Arabidopsis thaliana (Q9FNA2)
brenda
Cervelli, M.; Polticelli, F.; Fiorucci, L.; Angelucci, E.; Federico, R.; Mariottini, P.
Inhibition of acetylpolyamine and spermine oxidases by the polyamine analogue chlorhexidine
J. Enzyme Inhib. Med. Chem.
28
463-467
2013
Mus musculus (Q99K82)
-
brenda
Ahou, A.; Martignago, D.; Alabdallah, O.; Tavazza, R.; Stano, P.; Macone, A.; Pivato, M.; Masi, A.; Rambla, J.L.; Vera-Sirera, F.; Angelini, R.; Federico, R.; Tavladoraki, P.
A plant spermine oxidase/dehydrogenase regulated by the proteasome and polyamines
J. Exp. Bot.
65
1585-1603
2014
Arabidopsis thaliana (Q9SU79)
brenda
Hou, Z.; Liu, G.; Hou, L.; Wang, L.; Liu, X.
Regulatory function of polyamine oxidase-generated hydrogen peroxide in ethylene-induced stomatal closure in Arabidopsis thaliana
J. Integr. Agric.
12
251-262
2013
Arabidopsis thaliana (Q8H191)
-
brenda
Mo, H.; Wang, X.; Zhang, Y.; Zhang, G.; Zhang, J.; Ma, Z.
Cotton polyamine oxidase is required for spermine and camalexin signalling in the defence response to Verticillium dahliae
Plant J.
83
962-975
2015
Gossypium hirsutum
brenda
Kim, D.W.; Watanabe, K.; Murayama, C.; Izawa, S.; Niitsu, M.; Michael, A.J.; Berberich, T.; Kusano, T.
Polyamine oxidase 5 regulates Arabidopsis growth through Thermospermine oxidase activity
Plant Physiol.
165
1575-1590
2014
Arabidopsis thaliana (Q9SU79)
brenda
Leonetti, A.; Baroli, G.; Fratini, E.; Pietropaoli, S.; Marcoli, M.; Mariottini, P.; Cervelli, M.
Epileptic seizures and oxidative stress in a mouse model over-expressing spermine oxidase
Amino Acids
52
129-139
2020
Mus musculus (Q99K82), Mus musculus
brenda
Leonetti, A.; Cervoni, L.; Polticelli, F.; Kanamori, Y.; Yurtsever, Z.N.; Agostinelli, E.; Mariottini, P.; Stano, P.; Cervelli, M.
Spectroscopic and calorimetric characterization of spermine oxidase and its association forms
Biochem. J.
474
4253-4268
2017
Homo sapiens (Q9NWM0), Homo sapiens
brenda
Hu, T.; Sun, D.; Zhang, J.; Xue, R.; Janssen, H.L.A.; Tang, W.; Dong, L.
Spermine oxidase is upregulated and promotes tumor growth in hepatocellular carcinoma
Hepatol. Res.
48
967-977
2018
Homo sapiens (Q9NWM0), Homo sapiens
brenda
Reinoso-Sanchez, J.F.; Baroli, G.; Duranti, G.; Scaricamazza, S.; Sabatini, S.; Valle, C.; Morlando, M.; Casero, R.A.; Bozzoni, I.; Mariottini, P.; Ceci, R.; Cervelli, M.
Emerging role for linear and circular spermine oxidase RNAs in skeletal muscle physiopathology
Int. J. Mol. Sci.
21
8227
2020
Mus musculus (Q99K82), Mus musculus
brenda
Sun, L.; Yang, J.; Qin, Y.; Wang, Y.; Wu, H.; Zhou, Y.; Cao, C.
Discovery and antitumor evaluation of novel inhibitors of spermine oxidase
J. Enzyme Inhib. Med. Chem.
34
1140-1151
2019
Homo sapiens (Q9NWM0)
brenda
Di Paolo, M.L.; Cervelli, M.; Mariottini, P.; Leonetti, A.; Polticelli, F.; Rosini, M.; Milelli, A.; Basagni, F.; Venerando, R.; Agostinelli, E.; Minarini, A.
Exploring the activity of polyamine analogues on polyamine and spermine oxidase methoctramine, a potent and selective inhibitor of polyamine oxidase
J. Enzyme Inhib. Med. Chem.
34
740-752
2019
Mus musculus (Q99K82)
brenda
Sagor, G.H.M.; Inoue, M.; Kusano, T.; Berberich, T.
Expression profile of seven polyamine oxidase genes in rice (Oryza sativa) in response to abiotic stresses, phytohormones and polyamines
Physiol. Mol. Biol. Plants
27
1353-1359
2021
Oryza sativa Japonica Group (A0A0P0XM10), Oryza sativa Japonica Group (Q0J290), Oryza sativa Japonica Group (Q0J954), Oryza sativa Japonica Group (Q7XR46)
brenda
Uemura, T.; Takasaka, T.; Igarashi, K.; Ikegaya, H.
Spermine oxidase promotes bile canalicular lumen formation through acrolein production
Sci. Rep.
7
14841
2017
Homo sapiens (Q9NWM0)
brenda