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Literature summary extracted from

  • Birkholtz, L.; Joubert, F.; Neitz, A.W.; Louw, A.I.
    Comparative properties of a three-dimensional model of Plasmodium falciparum ornithine decarboxylase (2003), Proteins, 50, 464-473.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.17 alpha-difluoromethylornithine
-
 Plasmodium falciparum
4.1.1.17 CGP52622A 0.000064 mM, 50% inhibition Plasmodium falciparum
4.1.1.17 CGP54169A 0.000025 mM, 50% inhibition Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.17 L-ornithine Plasmodium falciparum
-
 putrescine + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.17 Plasmodium falciparum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.17 L-ornithine
-
 Plasmodium falciparum putrescine + CO2
-
 ?
4.1.1.17 L-ornithine bifunctional enzyme with ODC and S-adenosylmethionine decarboxylase activity, AdoMetDC component is located at the N-terminus and linked to ODC by approx. 180 amino acid residues Plasmodium falciparum putrescine + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.17 PfAdoMetDC-ODC
-
 Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.17 pyridoxal 5'-phosphate
-
 Plasmodium falciparum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.1.17 0.088
-
 alpha-difluoromethylornithine
-
 Plasmodium falciparum