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 (Comment) | Organism |
---|---|
AdoMetDC/ODC transcriptome, proteome and metabolome analysis, overview | Plasmodium falciparum |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | - |
- |
- |
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 | Comment | Organism |
---|---|---|
AdoMetDC/ODC | - |
Plasmodium falciparum |
ODC | - |
Plasmodium falciparum |
S-adenosylmethionine decarboxylase/ornithine decarboxylase | - |
Plasmodium falciparum |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
1 | - |
- |
Plasmodium falciparum | alpha-difluoromethylornithine |