Literature summary for 4.1.1.17 extracted from

Preeti, A.R.; Tapas, S.; Kumar, P.; Madhubala, R.; Tomar, S.
Structural insight into DFMO resistant ornithine decarboxylase from Entamoeba histolytica: an inkling to adaptive evolution (2013), PLoS ONE, 8, e53397.

Crystallization (Commentary)

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

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

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

Organism	UniProt	Comment	Textmining
Entamoeba histolytica	Q58P26	-	-

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	protein has conserved pyridoxal 5'-phosphate binding residues	Entamoeba histolytica

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Release 2023.1 (January 2023)