Crystallization (Comment) | Organism |
---|---|
C-terminally truncated enzyme, to 2.8 a resolution. Comparison with other ornithine decarboxylase homologs. Resistance to the irreversible inhibitor of ornithine decarboxylases, a-difluoromethylornithine, is due to substitution of key substrate binding residues in active site pocket. Additionally, a few more substitutions similar to antizyme inhibitor, a non-functional homologue of ornithine decarboxylases, are present | Entamoeba histolytica |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | enzyme from Entamoeba histolytica is resistant to the irreversible inhibitor of ornithine decarboxylases, a-difluoromethylornithine. crystallographic data | Entamoeba histolytica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Entamoeba histolytica | Q58P26 | - |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | protein has conserved pyridoxal 5'-phosphate binding residues | Entamoeba histolytica |