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Literature summary for 1.5.3.16 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
Search for more literature for 1.5.3.16

Cloned(Commentary)

Cloned (Comment) Organism
gene SMOX, phylogenetic analysis Homo sapiens
gene SMOX, phylogenetic analysis vertebrata
gene SMOX, phylogenetic analysis 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
0.19
-
 spermine isozyme SMO1, pH 8.0, temperature not specified in the publication Homo sapiens

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Homo sapiens
-
brain
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,16-diamino-4,8,13-triazahexadecane + O2 + H2O increased activity compared to spermine Homo sapiens ?
-
 ?
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 ?
-
 ?
N1-acetylspermine + O2 + H2O low activity Homo sapiens spermidine + N-acetyl-3-aminopropanal + H2O2
-
 ?
N1-acetylspermine + O2 + H2O low activity Mus musculus spermidine + N-acetyl-3-aminopropanal + H2O2
-
 ?
spermine + O2 + H2O
-
 Homo sapiens spermidine + 3-aminopropanal + H2O2
-
 ?
spermine + O2 + H2O
-
 vertebrata spermidine + 3-aminopropanal + H2O2
-
 ?
spermine + O2 + H2O
-
 Mus musculus spermidine + 3-aminopropanal + H2O2
-
 ?
spermine + O2 + H2O the enzyme is highly specific for spermine as substrate Mus musculus spermidine + 3-aminopropanal + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
SMO
-
 Homo sapiens
SMO
-
 vertebrata
SMO
-
 Mus musculus

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
6.6
-
 spermine isozyme SMO1, pH 8.0, temperature not specified in the publication Homo sapiens

Cofactor

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

General Information

General Information Comment Organism
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
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
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
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]

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