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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Expression
Expression on EC 1.5.3.16 - spermine oxidase
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ability of Tat to upregulate the activity of spermine oxidase, the polyamine catabolic enzyme that specifically oxidizes spermine, with the production of spermidine, H2O2, and 3-aminopropanal, through stimulation of the NMDA receptor, mechanism, overview
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both the expression level of SMO mRNA and SMO enzyme activity are significantly lower in breast cancer samples compared to nontumor samples
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expression of polyamine oxidase PAO4 is mildly induced by heat, cold, oxidative stress
expression of polyamine oxidase PAO7 is negatively regulated upon treatment with isopentenyl adenine, gibberellic acid and all polyamines
expression of polyamine oxidases PAO2 and PAO6 is negatively regulated upon indole acetic acid, isopentenyl adenine, gibberellic acid, abscisic acid
increased expression of spermine oxidase in ulcerative colitis and in prostate cancer and prostate intraepithelial neoplasia tissues. SMO expression is upregulated in gastritis tissues from patients with Helicobacter pylori infection, it is upregulated in both macrophages and epithelial cells
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positive regulation of AtPAO5 expression by polyamines at the transcriptional and post-transcriptional level
SMO is a highly inducible enzyme by a variety of stressful stimuli, including several antitumor polyamine analogues. Tumor-necrosis factor-alpha can induce H2O2 production via SMO gene upregulation
SMO transcript accumulation and enzymatic activity increase during C2C12 cell differentiation and correlate with the decrease of spermine content
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the expression of polyamine oxidases PAO2 and PAO6 is strongly induced upon wounding, drought, salinity, oxidative stress (H2O2), and exogenous application of jasmonic acid, spermidine, spermine, thermospermine
SMO is a highly inducible enzyme by a variety of stressful stimuli, including several antitumor polyamine analogues. Tumor-necrosis factor-alpha can induce H2O2 production via SMO gene upregulation
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SMO is a highly inducible enzyme by a variety of stressful stimuli, including several antitumor polyamine analogues. Tumor-necrosis factor-alpha can induce H2O2 production via SMO gene upregulation
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