Cloned (Comment) | Organism |
---|---|
isozymes SMOalpha and SMOmu, exon structures of murine SMO splice variants, overview | Mus musculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1,12-diaminododecane | - |
Mus musculus | |
bis(ethyl)norspermine | - |
Mus musculus | |
guazatine | - |
Mus musculus | |
additional information | poor inhibition by 1,8-diaminooctane | Mus musculus | |
N-prenylagmatine | - |
Mus musculus | |
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine | i.e. MDL72527 | Mus musculus | |
N1-ethyl-N11-(cyclopropyl)-methyl-4,8-diazaundecane | - |
Mus musculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.09 | - |
spermine | isozyme SMOalpha, pH 8.0, temperature not specified in the publication | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | isozymes SMO1 and SMO5 | Homo sapiens | 5737 | - |
cytoplasm | isozymes SMOalpha and SMOmu | Mus musculus | 5737 | - |
nucleus | isozyme SMOmu | Mus musculus | 5634 | - |
nucleus | isozymes SMO1 and SMO5 | Homo sapiens | 5634 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
spermine + O2 + H2O | Mus musculus | the enzyme specifically oxidizes spermine | spermidine + 3-aminopropanal + H2O2 | - |
? | |
spermine + O2 + H2O | Homo sapiens | the enzyme specifically oxidizes spermine | spermidine + 3-aminopropanal + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
splice variant isozymes SMO1 and SMO5 | - |
Mus musculus | - |
splice variant isozymes SMOalpha and SMOmu | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Mus musculus | - |
brain | - |
Homo sapiens | - |
C2C12 cell | - |
Mus musculus | - |
myoblast | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
spermine + O2 + H2O | - |
Mus musculus | spermidine + 3-aminopropanal + H2O2 | - |
? | |
spermine + O2 + H2O | - |
Homo sapiens | spermidine + 3-aminopropanal + H2O2 | - |
? | |
spermine + O2 + H2O | the enzyme specifically oxidizes spermine | Mus musculus | spermidine + 3-aminopropanal + H2O2 | - |
? | |
spermine + O2 + H2O | the enzyme specifically oxidizes spermine | Homo sapiens | spermidine + 3-aminopropanal + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SMO | - |
Mus musculus |
SMO | - |
Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4.5 | - |
spermine | isozyme SMOalpha, pH 8.0, temperature not specified in the publication | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
isozyme SMOalpha | Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavoprotein | Mus musculus | |
flavin | flavoprotein | Homo sapiens |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0004 | - |
guazatine | isozyme SMOalpha, pH 8.0, temperature not specified in the publication | Mus musculus | |
0.046 | - |
N-prenylagmatine | isozyme SMOalpha, pH 8.0, temperature not specified in the publication | Mus musculus | |
0.063 | - |
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine | isozyme SMOalpha, pH 8.0, temperature not specified in the publication | Mus musculus | |
0.085 | - |
N1-ethyl-N11-(cyclopropyl)-methyl-4,8-diazaundecane | isozyme SMOalpha, pH 8.0, temperature not specified in the publication | Mus musculus | |
0.38 | - |
bis(ethyl)norspermine | isozyme SMOalpha, pH 8.0, temperature not specified in the publication | Mus musculus | |
1 | - |
1,12-diaminododecane | isozyme SMOalpha, pH 8.0, temperature not specified in the publication | Mus musculus |
Organism | Comment | Expression |
---|---|---|
Mus musculus | 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 | up |
Homo sapiens | 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 | up |
General Information | Comment | Organism |
---|---|---|
evolution | isozyme SMOalpha displays a significant sequence similarity with the structurally characterized polyamine oxidase from maize | Mus musculus |
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 | Homo sapiens |
malfunction | SMO dysregulation can alter polyamine homeostasis affecting polyamine catabolism, which has been observed to be often associated with several disease states | Mus musculus |
metabolism | the enzyme is essential for polyamine homeostasis, which is mandatory for cellular life | Mus musculus |
metabolism | the enzyme is essential for polyamine homeostasis, which is mandatory for cellular life | Homo sapiens |
additional information | 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 | Mus musculus |
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 | Mus musculus |
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 | Homo sapiens |