Application | Comment | Organism |
---|---|---|
medicine | Snyder-Robinson syndrome (SRS) mutations drastically reduce spermine synthase activity and cause mild-to-moderate mental retardation, and may lead to a variety of other characteristics including a marfanoid habitus, skeletal defects, osteoporosis, and facial asymmetry, as well as hypotonia and movement disorders | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
G56S | point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers | Homo sapiens |
I150T | point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers | Homo sapiens |
additional information | yeast does not require spermine synthase since mutants in which this enzyme is deleted are viable and grow at a normal rate | Saccharomyces cerevisiae |
V132G | point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers | Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
41000 | - |
2 * 41000, each monomer has three domains: an N-terminal domain, which contains most of the dimer contacts; a central domain made up of four beta-strands that serves as a lid for the C-terminal domain, and a C-terminal catalytic domain | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mus musculus | spermine synthase is clearly essential for mammalia | ? | - |
? | |
additional information | Homo sapiens | spermine synthase is clearly essential for normal development in humans | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Monosiga brevicollis | - |
- |
- |
Mus musculus | - |
- |
- |
no activity in Caenorhabditis elegans | - |
- |
- |
no activity in Hydra magnipapillata | - |
- |
- |
Saccharomyces cerevisiae | - |
only fungi where spermine synthase is found is the Saccharomycotina class of the Ascomycota | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
H2N(CH2)3NH(CH2)4NH2 + S-adenosyl 3-(methylthio)propylamine | - |
Homo sapiens | H2N(CH2)3NH(CH2)4NH(CH2)3NH2 + S-methyl-5'-thioadenosine | - |
? | |
additional information | spermine synthase is clearly essential for mammalia | Mus musculus | ? | - |
? | |
additional information | spermine synthase is clearly essential for normal development in humans | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Mus musculus |
dimer | - |
Saccharomyces cerevisiae |
dimer | - |
Monosiga brevicollis |
dimer | 2 * 41000, each monomer has three domains: an N-terminal domain, which contains most of the dimer contacts; a central domain made up of four beta-strands that serves as a lid for the C-terminal domain, and a C-terminal catalytic domain | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
SMS | - |
Mus musculus |
SMS | - |
Homo sapiens |
SMS | - |
Saccharomyces cerevisiae |
SMS | - |
Monosiga brevicollis |
spermine synthase | highly specific aminopropyltransferase | Mus musculus |
spermine synthase | highly specific aminopropyltransferase | Homo sapiens |
spermine synthase | highly specific aminopropyltransferase | Saccharomyces cerevisiae |
spermine synthase | highly specific aminopropyltransferase | Monosiga brevicollis |
SpmSyn | - |
Mus musculus |
SpmSyn | - |
Homo sapiens |
SpmSyn | - |
Saccharomyces cerevisiae |
SpmSyn | - |
Monosiga brevicollis |