title: Ornithine decarboxylase in Trypanosoma brucei brucei: evidence for selective toxicity of difluoromethylornithine.
abstract: Activity of ornithine decarboxylase, the major rate limiting enzyme of polyamine biosynthesis, was determined in bloodstream trypomastigotes of Trypanosoma brucei brucei. The enzyme required pyridoxal-5'-phosphate, dithiothreitol and EDTA for optimal activity. Several properties of the enzyme were investigated and compared to the mammalian enzyme. Most notably, the parasite enzyme was greater than 60-fold more sensitive to the inhibitor DL-alpha-difluoromethylornithine than its mammalian counterpart, thus making it an attractive target for chemotherapy.
mesh_terms: D000818:Animals; D002262:Carboxy-Lyases / Q000378:metabolism*; D000518:Eflornithine; D004790:Enzyme Induction; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009952:Ornithine / Q000031:analogs & derivatives* / Q000494:pharmacology; D009955:Ornithine Decarboxylase / Q000378:metabolism*; D065108:Ornithine Decarboxylase Inhibitors; D011073:Polyamines / Q000494:pharmacology; D014346:Trypanosoma brucei brucei / Q000201:enzymology*
chemical_list: D065108:Ornithine Decarboxylase Inhibitors; D011073:Polyamines; C025025:alpha-methylornithine; D009952:Ornithine; D002262:Carboxy-Lyases; D009955:Ornithine Decarboxylase; D000518:Eflornithine