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Literature summary extracted from

  • Zhang, Z.; Martiny, V.; Lagorce, D.; Ikeguchi, Y.; Alexov, E.; Miteva, M.A.
    Rational design of small-molecule stabilizers of spermine synthase dimer by virtual screening and free energy-based approach (2014), PLoS ONE, 9, e110884.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.22 G56S the mutation destabilizes the enzyme homodimer and thus abolishes enzymatic activity 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 S-adenosyl 3-(methylthio)propylamine + spermidine Homo sapiens
-
 S-methyl-5'-thioadenosine + spermine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.22 Homo sapiens P52788
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.22 TALON affinity resin column chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.22 S-adenosyl 3-(methylthio)propylamine + spermidine
-
 Homo sapiens S-methyl-5'-thioadenosine + spermine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.22 homodimer x-ray crystallography Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.5.1.22 SMS
-
 Homo sapiens