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Literature summary for 4.1.1.17 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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-ornithine
-
Plasmodium falciparum putrescine + CO2
-
?
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

Synonyms Comment Organism
PfAdoMetDC-ODC
-
Plasmodium falciparum

Cofactor

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

Ki Value [mM]

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