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Ornithine Decarboxylase in Trypanosoma brucei brucei : Evidence for Selective Toxicity of Difluoromethylornithine 1
Author(s) -
GAROFALO JOANNE,
BACCHHI C. J.,
McLAUGHLIN SUSAN DITTUS,
MOCKENHAUPT DIANE,
TRUEBA GENEROSA,
HUTNER S. H.
Publication year - 1982
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1982.tb05418.x
Subject(s) - trypanosoma brucei , ornithine decarboxylase , dithiothreitol , eflornithine , enzyme , biochemistry , biology , enzyme assay , chemistry , microbiology and biotechnology , gene
. 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 >60‐fold more sensitive to the inhibitor DL‐α‐difluoromethylornithine than its mammalian counterpart, thus making it an attractive target for chemotherapy.