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Literature summary for 4.1.1.50 extracted from

  • van Brummelen, A.C.; Olszewski, K.L.; Wilinski, D.; Llinas, M.; Louw, A.I.; Birkholtz, L.M.
    Co-inhibition of Plasmodium falciparum S-adenosylmethionine decarboxylase/ornithine decarboxylase reveals perturbation-specific compensatory mechanisms by transcriptome, proteome and metabolome analyses (2008), J. Biol. Chem., 284, 4635-4646.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
MDL73811 i.e. 5'-[[(Z)-4-amino-2-butenyl]methylamino]-5'-deoxyadenosine, complete inhibition at 0.005 mM Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
schizont
-
Plasmodium falciparum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine
-
Plasmodium falciparum (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
-
?

Synonyms

Synonyms Comment Organism
AdoMetDC
-
Plasmodium falciparum
AdoMetDC/ODC ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) form a single bifunctional protein in Plasmodium falciparum Plasmodium falciparum
S-Adenosylmethionine decarboxylase
-
Plasmodium falciparum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Plasmodium falciparum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.001
-
-
Plasmodium falciparum MDL73811