Open AccessBiochemical characterization of a low‐affinity arginine permease from the parasite Trypanosoma cruzi
Author(s) -
Canepa Gaspar E,
Silber Ariel M,
Bouvier León A,
Pereira Claudio A
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2004.tb09630.x
Subject(s) - trypanosoma cruzi , arginine , permease , biochemistry , transporter , amino acid , trypanosoma , biology , methionine , parasite hosting , chemistry , gene , virology , world wide web , computer science
Trypanosoma cruzi , the etiological agent of Chagas disease, uses arginine for several metabolic processes, including energy reserves management. In the present work, a novel low‐affinity arginine transport system has been studied. Maximum velocity (97 pmol min −1 per 10 7 cells), and an estimate for the apparent K m value (350 μM) of this arginine transporter, were 6‐fold and 80‐fold higher respectively, when compared with the previously described high‐affinity arginine transport system. This transport activity seems to be H + ‐mediated, presents a broad specificity by other amino acids such as methionine, and is regulated along the parasite growth curve and life cycle.