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Literature summary for 2.5.1.22 extracted from

  • Pegg, A.E.; Michael, A.J.
    Spermine synthase (2010), Cell. Mol. Life Sci., 67, 113-121.
    View publication on PubMedView publication on EuropePMC

Application

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

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 [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/ Products (Substrates)

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

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 and Products (Substrate)

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

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

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