1.5.3.16: spermine oxidase
This is an abbreviated version!
For detailed information about spermine oxidase, go to the full flat file.
Word Map on EC 1.5.3.16
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1.5.3.16
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polyamine
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putrescine
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acetylpolyamine
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back-conversion
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n1-acetylspermine
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n1-acetylpolyamine
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3-aminopropanal
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acrolein
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benspm
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medicine
- 1.5.3.16
- polyamine
- putrescine
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acetylpolyamine
-
back-conversion
- n1-acetylspermine
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n1-acetylpolyamine
- 3-aminopropanal
- acrolein
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benspm
- medicine
Reaction
Synonyms
AtPAO1, AtPAO4, AtPAO5, EC 1.5.3.11, Fms1 protein, GhPAO, hSMO, MmSMO, mSMO, mSMOalpha, mSMOmu, PAO, PAO1, PAO4, PAO5, PAO6, PAO7, PAOh1, PAOh1/SMO, SelPAO5, SMO, SMO(PAOh1), SMO/PAOh1, SMO5, SMOX, spermine oxidase, Spm oxidase, thermospermine oxidase
ECTree
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General Information
General Information on EC 1.5.3.16 - spermine oxidase
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evolution
malfunction
metabolism
physiological function
additional information
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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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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
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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
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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
spermine oxidase as an important positive regulator of muscle gene expression and fiber size
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
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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