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Literature summary for 1.5.3.16 extracted from

  • Cervelli, M.; Amendola, R.; Polticelli, F.; Mariottini, P.
    Spermine oxidase: ten years after (2012), Amino Acids, 42, 441-450.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
isozymes SMOalpha and SMOmu, exon structures of murine SMO splice variants, overview Mus musculus

Inhibitors

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 [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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens
-
splice variant isozymes SMO1 and SMO5
-
Mus musculus
-
splice variant isozymes SMOalpha and SMOmu
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Mus musculus
-
brain
-
Homo sapiens
-
C2C12 cell
-
Mus musculus
-
myoblast
-
Mus musculus
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
SMO
-
Mus musculus
SMO
-
Homo sapiens

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
isozyme SMOalpha Mus musculus

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Mus musculus
flavin flavoprotein Homo sapiens

Ki Value [mM]

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

Expression

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

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