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Literature summary for 4.1.1.50 extracted from

  • Xiong, H.; Stanley, B.A.; Pegg, A.E.
    Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase (1999), Biochemistry, 38, 2462-2470.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C82A reduced enzymic activity, no inhibition by iodoacetic acid Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
iodoacetic acid
-
Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
8900
-
x * 39600, proenzyme, x * 30600, alpha, + x * 8900, beta, SDS-PAGE Homo sapiens
30600
-
x * 39600, proenzyme, x * 30600, alpha, + x * 8900, beta, SDS-PAGE Homo sapiens
39600
-
x * 39600, proenzyme, x * 30600, alpha, + x * 8900, beta, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
recombinant protein, expression in Escherichia coli
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification proenzyme of 39600 Da is cleaved to alpha subunit, 30600 Da, and beta subunit, 8900 Da Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine = S-adenosyl 3-(methylsulfanyl)propylamine + CO2 mechanism Homo sapiens

Subunits

Subunits Comment Organism
? x * 39600, proenzyme, x * 30600, alpha, + x * 8900, beta, SDS-PAGE Homo sapiens