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Literature summary extracted from

  • Da'dara, A.A.; Walter, R.D.
    Molecular and biochemical characterization of S-adenosylmethionine decarboxylase from free-living nematode Caenorhabditis elegans (1998), Biochem. J., 336, 545-550.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.1.1.50 pharmacology potentially important drug target for the chemotherapy of proliferative and parasitic diseases Caenorhabditis elegans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.50 10000
-
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE Caenorhabditis elegans
4.1.1.50 32000
-
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE Caenorhabditis elegans

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.50 Caenorhabditis elegans O02655
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.1.1.50 proteolytic modification alpha-subunit, 32000 Da, and beta-subunit, 10000 Da, are derived from cleavage of the proenzyme. The mRNA has an unusually long 5'-untranslated region of 477 nucleotides. This region has a small open reading frame, which can encode a putative peptide of 17000 residues Caenorhabditis elegans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.50 S-adenosyl-L-methionine
-
Caenorhabditis elegans (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.50 tetramer 2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE Caenorhabditis elegans