IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
artículos
Título:
Characterization ofTrypanosoma cruzi L-cysteinetransport
Autor/es:
CANEPA, GE.; BOUVIER, LA.; MIRANDA, MR.; UTTARO, ANTONIO D.; PEREIRA, CA.
Revista:
FEMS MICROBIOLOGY LETTERS
Editorial:
Blackwell Publishing Ltd.
Referencias:
Año: 2009 vol. 292 p. 27 - 32
ISSN:
0378-1097
Resumen:
L-Cysteine and methionine are unique amino acids that act as sulfur donors in all organisms. In the specific case of Trypanosomatids, L-cysteine is particularly relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi organisms. In the specific case of Trypanosomatids, L-cysteine is particularly relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi organisms. In the specific case of Trypanosomatids, L-cysteine is particularly relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi -Cysteine and methionine are unique amino acids that act as sulfur donors in all organisms. In the specific case of Trypanosomatids, L-cysteine is particularly relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzi L-cysteine is particularly relevant as a substrate in the synthesis of trypanothione. Although it can be synthesized de novo, L-cysteine is actively transported in Trypanosoma cruzide novo, L-cysteine is actively transported in Trypanosoma cruzi epimastigote cells. L-Cysteine uptake is highly specific; none of the amino acids assayed yield significant differences in terms of transport rates. L-Cysteine is transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a assayed yield significant differences in terms of transport rates. L-Cysteine is transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a assayed yield significant differences in terms of transport rates. L-Cysteine is transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a L-Cysteine uptake is highly specific; none of the amino acids assayed yield significant differences in terms of transport rates. L-Cysteine is transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a transported by epimastigote cells with a calculated apparent Km of 49.5 uM and a L-Cysteine is transported by epimastigote cells with a calculated apparent Km of 49.5 uM and aKm of 49.5 uM and a Vmax of about 13 pmol min1 per 107 cells. This transport is finely regulated by amino acid starvation, extracellular pH, and between the parasite growth phases. In addition, L-cysteine is incorporated post-translationally into proteins, suggesting its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. amino acid starvation, extracellular pH, and between the parasite growth phases. In addition, L-cysteine is incorporated post-translationally into proteins, suggesting its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. amino acid starvation, extracellular pH, and between the parasite growth phases. In addition, L-cysteine is incorporated post-translationally into proteins, suggesting its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. max of about 13 pmol min1 per 107 cells. This transport is finely regulated by amino acid starvation, extracellular pH, and between the parasite growth phases. In addition, L-cysteine is incorporated post-translationally into proteins, suggesting its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. L-cysteine is incorporated post-translationally into proteins, suggesting its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico. were predicted in silico. were predicted in silico. L-cysteine were predicted in silico.in silico.