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Literature summary 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

EC Number Application Comment Organism
2.5.1.22 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

EC Number Protein Variants Comment Organism
2.5.1.22 G56S point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers Homo sapiens
2.5.1.22 I150T point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers Homo sapiens
2.5.1.22 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
2.5.1.22 V132G point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.22 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.22 additional information Mus musculus spermine synthase is clearly essential for mammalia ?
-
?
2.5.1.22 additional information Homo sapiens spermine synthase is clearly essential for normal development in humans ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.22 Homo sapiens
-
-
-
2.5.1.22 Monosiga brevicollis
-
-
-
2.5.1.22 Mus musculus
-
-
-
2.5.1.22 no activity in Caenorhabditis elegans
-
-
-
2.5.1.22 no activity in Hydra magnipapillata
-
-
-
2.5.1.22 Saccharomyces cerevisiae
-
only fungi where spermine synthase is found is the Saccharomycotina class of the Ascomycota
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.22 H2N(CH2)3NH(CH2)4NH2 + S-adenosyl 3-(methylthio)propylamine
-
Homo sapiens H2N(CH2)3NH(CH2)4NH(CH2)3NH2 + S-methyl-5'-thioadenosine
-
?
2.5.1.22 additional information spermine synthase is clearly essential for mammalia Mus musculus ?
-
?
2.5.1.22 additional information spermine synthase is clearly essential for normal development in humans Homo sapiens ?
-
?

Subunits

EC Number Subunits Comment Organism
2.5.1.22 dimer
-
Mus musculus
2.5.1.22 dimer
-
Saccharomyces cerevisiae
2.5.1.22 dimer
-
Monosiga brevicollis
2.5.1.22 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

EC Number Synonyms Comment Organism
2.5.1.22 SMS
-
Mus musculus
2.5.1.22 SMS
-
Homo sapiens
2.5.1.22 SMS
-
Saccharomyces cerevisiae
2.5.1.22 SMS
-
Monosiga brevicollis
2.5.1.22 spermine synthase highly specific aminopropyltransferase Mus musculus
2.5.1.22 spermine synthase highly specific aminopropyltransferase Homo sapiens
2.5.1.22 spermine synthase highly specific aminopropyltransferase Saccharomyces cerevisiae
2.5.1.22 spermine synthase highly specific aminopropyltransferase Monosiga brevicollis
2.5.1.22 SpmSyn
-
Mus musculus
2.5.1.22 SpmSyn
-
Homo sapiens
2.5.1.22 SpmSyn
-
Saccharomyces cerevisiae
2.5.1.22 SpmSyn
-
Monosiga brevicollis