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Literature summary extracted from

  • Pegg, A.E.; Wang, X.; Schwartz, C.E.; McCloskey, D.E.
    Spermine synthase activity affects the content of decarboxylated S-adenosylmethionine (2011), Biochem. J., 433, 139-144.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.22 expression of human spermine synthase in CAGSMS line 8 mice from a composite CMV-IE enhancer/chicken beta-actin promoter. Transgenic expression of spermine synthase in the Gy mice reverse all of the increases in dcAdoMet content and AdoMetDC Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.5.1.22 cytosol
-
 Mus musculus 5829
-
2.5.1.22 cytosol
-
 Homo sapiens 5829
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.22 S-adenosylmethioninamine + spermidine Mus musculus decarboxylated S-adenosylmethionine is an essential intermediate in the synthesis of polyamines S-methyl-5'-thioadenosine + spermine
-
 ?
2.5.1.22 S-adenosylmethioninamine + spermidine Homo sapiens decarboxylated S-adenosylmethionine is an essential intermediate in the synthesis of polyamines S-methyl-5'-thioadenosine + spermine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.22 Homo sapiens
-
-
-
2.5.1.22 Mus musculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.22 brain
-
 Mus musculus
-
2.5.1.22 cell culture
-
 Homo sapiens
-
2.5.1.22 kidney
-
 Mus musculus
-
2.5.1.22 liver
-
 Mus musculus
-
2.5.1.22 lymphoblast from patients with Snyder-Robinson syndrome and non-affected individuals Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.22 S-adenosylmethioninamine + spermidine
-
 Mus musculus S-methyl-5'-thioadenosine + spermine
-
 ?
2.5.1.22 S-adenosylmethioninamine + spermidine
-
 Homo sapiens S-methyl-5'-thioadenosine + spermine
-
 ?
2.5.1.22 S-adenosylmethioninamine + spermidine decarboxylated S-adenosylmethionine is an essential intermediate in the synthesis of polyamines Mus musculus S-methyl-5'-thioadenosine + spermine
-
 ?
2.5.1.22 S-adenosylmethioninamine + spermidine decarboxylated S-adenosylmethionine is an essential intermediate in the synthesis of polyamines Homo sapiens S-methyl-5'-thioadenosine + spermine
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.22 7.5
-
 assay at Homo sapiens

General Information

EC Number General Information Comment Organism
2.5.1.22 malfunction cells derived from patients with Snyder-Robinson syndrome, a rare X-linked recessive human disease caused by SMS gene mutations that greatly reduce the content of spermine synthase, show an increase in decarboxylated S-adenosylmethionine Homo sapiens
2.5.1.22 malfunction in Gy mice, which lack spermine synthase activity, the content of dcAdoMet is significantly increased by 10-30fold in liver, brain and kidney and by 150fold in heart. Transgenic expression of spermine synthase in the Gy mice reverses all of the increases in dcAdoMet content and AdoMetDC, phenotypes, overview Mus musculus
2.5.1.22 physiological function inverse relationship between the amount of spermine synthase protein and the content of decarboxylated S-adenosylmethionine. In mice lacking spermine synthase occurs a large increase in decarboxylated S-adenosylmethionine, dcAdoMet, overexpression of human spermine synthase reduces the amount of this nucleoside, Content of AdoMet and dcAdoMet in cultured lymphoblasts from control and Snyder-Robinson syndrome patients Homo sapiens