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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

Reaction

spermine
+
O2
+
H2O
=
spermidine
+
3-aminopropanal
+
H2O2

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

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.3 With oxygen as acceptor
                1.5.3.16 spermine oxidase

Expression

Expression on EC 1.5.3.16 - spermine oxidase

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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
both the expression level of SMO mRNA and SMO enzyme activity are significantly lower in breast cancer samples compared to nontumor samples
-
expression is down-regulated by dehydration stress
expression is up-regulated by thermospermine treatment
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
-
no induction of SMO activity by N-alkylated polyamine analogues
-
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
-
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