Open AccessOn the regulatory properties of the pyruvate kinase from Trypanosoma cruzi epimastigotes
Author(s) -
Cazzulo Juan José,
Cazzulo Franke María Cristina,
Franke de Cazzulo Berta Maria
Publication year - 1989
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.1574-6968.1989.tb03121.x
Subject(s) - trypanosoma cruzi , pyruvate kinase , chemistry , biochemistry , biology , enzyme , glycolysis , parasite hosting , world wide web , computer science
The pyruvate kinase from Trypanosoma cruzi epimastigotes was activated by fructose 2,6‐diphosphate ((A) 0.5 = 0.17 μ M), through a decrease in (S) 0.5 and an increase in V max for both substrates. The enzyme was 50% inhibited by 0.9 mM ATP or 0.5 mM Pi in the presence of 30 mM MgC12; these inhibitions were completely counteracted by 1.5 μM fructose 2,6‐diphosphate. Both facts suggest that the effects are allosteric, and not due to chelation.