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Screening of Substrate Analogs as Potential Enzyme Inhibitors for the Arginine Kinase of Trypanosoma cruzi
Author(s) -
PEREIRA CLAUDIO A.,
ALONSO GUILLERMO D.,
IVAUDI SOLEDAD,
BOUVIER LEÓN A.,
TORRES HÉCTOR N.,
FLAWIÁ MIRTHA M.
Publication year - 2003
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.2003.tb00247.x
Subject(s) - arginine kinase , arginine , canavanine , agmatine , trypanosoma cruzi , biology , biochemistry , kinase , enzyme , microbiology and biotechnology , amino acid , parasite hosting , world wide web , computer science
. Arginine kinase catalyzes the transphosphorylation between phosphoarginine and ADP. Phosphoarginine is involved in temporal ATP buffering and inorganic phosphate regulation. Trypanosoma cruzi arginine kinase phosphorylates only L‐arginine (specific activity 398.9 mUE‐min −1 mg −1 ), and is inhibited by the arginine analogs, agmatine, canavanine, nitroarginine, and homoarginine. Canavanine and homoarginine also produce a significant inhibition of the epimastigote culture growth (79.7% and 55.8%, respectively). Inhibition constants were calculated for canavanine and homoarginine (7.55 and 6.02 mM, respectively). In addition, two novel guanidino kinase activities were detected in the epimastigote soluble extract. The development of the arginine kinase inhibitors of T. cruzi could be an important feature because the phosphagens biosynthetic pathway in trypanosomatids is different from the one in their mammalian hosts.