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Literature summary extracted from

  • Cervelli, M.; Salvi, D.; Polticelli, F.; Amendola, R.; Mariottini, P.
    in the evolutionary framework of spermine oxidase (2013), J. Mol. Evol., 76, 365-370.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.3.16 gene SMOX, phylogenetic analysis Homo sapiens
1.5.3.16 gene SMOX, phylogenetic analysis vertebrata
1.5.3.16 gene SMOX, phylogenetic analysis Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.3.16 0.09
-
 spermine isozyme SMOalpha, pH 8.0, temperature not specified in the publication Mus musculus
1.5.3.16 0.19
-
 spermine isozyme SMO1, pH 8.0, temperature not specified in the publication Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.3.16 cytoplasm isozymes SMOalpha and SMOmu Homo sapiens 5737
-
1.5.3.16 cytoplasm isozymes SMOalpha and SMOmu Mus musculus 5737
-
1.5.3.16 nucleus isozyme SMOmu Homo sapiens 5634
-
1.5.3.16 nucleus isozyme SMOmu Mus musculus 5634
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.3.16 spermine + O2 + H2O Homo sapiens
-
 spermidine + 3-aminopropanal + H2O2
-
 ?
1.5.3.16 spermine + O2 + H2O vertebrata
-
 spermidine + 3-aminopropanal + H2O2
-
 ?
1.5.3.16 spermine + O2 + H2O Mus musculus
-
 spermidine + 3-aminopropanal + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.16 Homo sapiens
-
 gene SMOX, splice variant isozymes SMO1 and SMO5
-
1.5.3.16 Mus musculus Q99K82 gene SMOX, splice variant isozymes SMOalpha and SMOmu
-
1.5.3.16 vertebrata
-
 gene SMOX
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.3.16 brain
-
 Homo sapiens
-
1.5.3.16 brain
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.16 1,16-diamino-4,8,13-triazahexadecane + O2 + H2O increased activity compared to spermine Homo sapiens ?
-
 ?
1.5.3.16 additional information significant activity of this enzyme also on other linear tetramines (i.e. homospermine and N-butylated spermine) and, more importantly, on linear pentamines Homo sapiens ?
-
 ?
1.5.3.16 N1-acetylspermine + O2 + H2O low activity Homo sapiens spermidine + N-acetyl-3-aminopropanal + H2O2
-
 ?
1.5.3.16 N1-acetylspermine + O2 + H2O low activity Mus musculus spermidine + N-acetyl-3-aminopropanal + H2O2
-
 ?
1.5.3.16 spermine + O2 + H2O
-
 Homo sapiens spermidine + 3-aminopropanal + H2O2
-
 ?
1.5.3.16 spermine + O2 + H2O
-
 vertebrata spermidine + 3-aminopropanal + H2O2
-
 ?
1.5.3.16 spermine + O2 + H2O
-
 Mus musculus spermidine + 3-aminopropanal + H2O2
-
 ?
1.5.3.16 spermine + O2 + H2O the enzyme is highly specific for spermine as substrate Mus musculus spermidine + 3-aminopropanal + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.5.3.16 SMO
-
 Homo sapiens
1.5.3.16 SMO
-
 vertebrata
1.5.3.16 SMO
-
 Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.3.16 4.5
-
 spermine isozyme SMOalpha, pH 8.0, temperature not specified in the publication Mus musculus
1.5.3.16 6.6
-
 spermine isozyme SMO1, pH 8.0, temperature not specified in the publication Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.16 FAD dependent on Homo sapiens
1.5.3.16 FAD dependent on vertebrata
1.5.3.16 FAD dependent on Mus musculus

General Information

EC Number General Information Comment Organism
1.5.3.16 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 Homo sapiens
1.5.3.16 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 Mus musculus
1.5.3.16 evolution 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 vertebrata
1.5.3.16 additional information 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 Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.5.3.16 0.8
-
 N1-acetylspermine isozyme SMO1, pH 8.0, temperature not specified in the publication Homo sapiens
1.5.3.16 37
-
 N1-acetylspermine pH 8.0, temperature not specified in the publication Mus musculus