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Literature summary for 4.1.1.17 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
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Application

Application Comment Organism
medicine polyamine-depletion as an antimalarial strategy, cytostasis caused by the co-inhibition of S-adenosylmethionine decarboxylase/ornithine decarboxylase in Plasmodium falciparum Plasmodium falciparum

Cloned(Commentary)

Cloned (Comment) Organism
AdoMetDC/ODC transcriptome, proteome and metabolome analysis, overview Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
alpha-difluoromethylornithine
-
 Plasmodium falciparum
additional information ODC inhibition decreases putrescine levels, AdoMetDC inhibition decreases the levels of both spermidine and spermine Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-ornithine Plasmodium falciparum the organism responds to alleviate the detrimental effects of polyamine depletion via regulation of its transcriptome and subsequently the proteome and metabolome, AdoMetDC/ODC transcriptome, proteome and metabolome analysis, overview putrescine + CO2
-
 ?
additional information Plasmodium falciparum in Plasmodium falciparum the two rate-limiting enzymes of polyamine biosynthesis, ornithine decarboxylase, ODC, and S-adenosylmethionine decarboxylase, ADoMetDC EC 4.1.1.50, form a single bifunctional protein, AdoMetDC/ODC ?
-
 ?

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 the organism responds to alleviate the detrimental effects of polyamine depletion via regulation of its transcriptome and subsequently the proteome and metabolome, AdoMetDC/ODC transcriptome, proteome and metabolome analysis, overview Plasmodium falciparum putrescine + CO2
-
 ?
additional information in Plasmodium falciparum the two rate-limiting enzymes of polyamine biosynthesis, ornithine decarboxylase, ODC, and S-adenosylmethionine decarboxylase, ADoMetDC EC 4.1.1.50, form a single bifunctional protein, AdoMetDC/ODC Plasmodium falciparum ?
-
 ?

Synonyms

Synonyms Comment Organism
AdoMetDC/ODC
-
 Plasmodium falciparum
ODC
-
 Plasmodium falciparum
S-adenosylmethionine decarboxylase/ornithine decarboxylase
-
 Plasmodium falciparum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1
-
-
 Plasmodium falciparum alpha-difluoromethylornithine