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 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 | 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 | 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 | 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 | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Homo sapiens | - |
brain | - |
Mus musculus | - |
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 | Comment | Organism |
---|---|---|
SMO | - |
Homo sapiens |
SMO | - |
vertebrata |
SMO | - |
Mus musculus |
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 | Comment | Organism | Structure |
---|---|---|---|
FAD | dependent on | Homo sapiens | |
FAD | dependent on | vertebrata | |
FAD | dependent on | Mus musculus |
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 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 |