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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
?
-
-
-
-
?
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-acetylspermine + O2 + H2O
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
N1-acetylspermine + O2 + H2O
spermidine + N-acetyl-3-aminopropanal + H2O2
-
low activity
-
-
?
N1-ethyl-spermine + O2 + H2O
spermidine + N-ethyl-3-aminopropanal + H2O2
-
good substrate
-
-
?
N1-monoethylspermine + O2 + H2O
spermidine + ?
98% of the activity with spermine
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
additional information
?
-
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
-
the ethyl substituent that retains the amine as positively charged, strongly accelerates the reaction velocity
-
-
?
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
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
-
-
?
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
-
-
?
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bis(ethyl)norspermine
-
structure modeling analysis of complex formed with SMO
MDL-72527
0.2 mM, 41% inhibition
N-(3-aminopropyl)-N-2,3-butadienyl-1,4-butanediamine
potent inhibition
N-(3-[[3-(dimethylamino)propyl]amino]propyl)-8-quinolinecarboxamide
i.e. SI-4650, inhibits spermine oxidase enzyme activity, increases substrate spermine content and reduces product spermidine content. Treatment suppresses cell proliferation and migration, the inhibitor causes cell cycle arrest, induces cell apoptosis, and promotes autophagy
-
N-[3-(2,3-butadienylamino)propyl]-1,4-butanediamine
moderate inhibition
N1,N11-diethylnorspermine
0.2 mM, 21% inhibition
N1,N12-diethylspermine
0.2 mM, 15% inhibition
N1,N14-diethylhomospermine
0.2 mM, 49% inhibition
N1,N4-bis(2,3-butadienyl)-1,4 butanediamine
-
i.e. MDL72527
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine
N1-(n-octanesulfonyl)spermine
0.2 mM, 86% inhibition
N1-ethyl-N11-(cyclopropyl)-methyl-4,8-diazaundecane
-
structure modeling analysis of complex formed with SMO
SL-11144
potent inhibitor of PAOh1/SMO, IC50 below 0.01 mM
SL-11150
potent inhibitor of PAOh1/SMO, IC50 below 0.01 mM
SL-11158
potent inhibitor of PAOh1/SMO, IC50 below 0.01 mM
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine
i.e. MDL72527
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine
i.e. MDL72527, 0.25 mM, more than 95% inhibition
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine
-
i.e. MDL72527, partial inhibition
spermidine
0.2 mM, 41% inhibition
additional information
no inhibition by N1-ethyl-N11-(cycloheptyl)methyl-4,8,diazaundecane
-
additional information
-
no inhibition by N1-ethyl-N11-(cycloheptyl)methyl-4,8,diazaundecane
-
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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
-
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
malfunction
-
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
metabolism
-
SMO is a key enzyme of polyamine catabolism, metabolism of N-alkylated spermine analogues by polyamine and spermine oxidases, overview
metabolism
-
the enzyme is essential for polyamine homeostasis, which is mandatory for cellular life
metabolism
-
the enzyme is involved in polyamine catabolic pathways, overview
metabolism
the enzyme is involved in polyamine catabolism
physiological function
-
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
-
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
-
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
the enzyme is a regulator of macrophage host response to Helicobacter pylori. It enhances antimicrobial nitric oxide generation by depletion of spermine
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
-
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
-
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
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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.
61
5370-5373
2001
Homo sapiens (Q9NWM0)
brenda
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
605-611
2003
Homo sapiens (Q9NWM0), Homo sapiens
brenda
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
Biochem. J.
367
665-675
2002
Homo sapiens (Q9NWM0), Homo sapiens, Mus musculus (Q99K82), Mus musculus
brenda
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
Biochem. J.
386
543-547
2005
Homo sapiens
brenda
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
Cancer Res.
66
11125-11130
2006
Homo sapiens
brenda
Murray-Stewart, T.; Wang, Y.; Goodwin, A.; Hacker A.; Meeker, A.; casero, R.A.
Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology
FEBS J.
275
2795-2806
2008
Homo sapiens, Homo sapiens (Q9NWM0)
brenda
Pledgie, A.; Huang, Y.; Hacker, A.; Zhang, Z.; Woster, P.M.; Davidson, N.E.; Casero, R.A.
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
J. Biol. Chem.
280
39843-39851
2005
Homo sapiens
brenda
Järvinen, A.; Grigorenko, N.; Khomutov, A.R.; Hyvönen, M.T.; Uimari, A.; Vepsäläinen, J.; Sinervirta, R.; Keinänen, T.A.; Vujcic, S.; Alhonen, L.; Porter, C.W.; Jänne, J.
Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural polyamines.
J. Biol. Chem.
280
6595-6601
2005
Homo sapiens
brenda
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
766-772
2008
Homo sapiens
brenda
Adachi, M.S.; Juarez, P.R.; Fitzpatrick, P.F.
Mechanistic studies of human spermine oxidase: kinetic mechanism and pH effects
Biochemistry
49
386-392
2010
Homo sapiens
brenda
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
2010
Homo sapiens, Mus musculus
brenda
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
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
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
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
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
Homo sapiens (Q9NWM0), Homo sapiens, Mus musculus (Q99K82), Mus musculus
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
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
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
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