CharacterizationofTrypanosoma cruzi L-cysteine transport mechanismsand theiradaptive regulation

Abstract

disease. 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 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 mM and a Vmax of about 13 pmolmin 1 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, suggest-ing its role in iron–sulfur core formation. Finally, the metabolic fates of L-cysteine were predicted in silico

Similar works

Full text

thumbnail-image
oai:CiteSeerX.psu:10.1.1.905.1986Last time updated on 11/1/2017

This paper was published in CiteSeerX.

Having an issue?

Is data on this page outdated, violates copyrights or anything else? Report the problem now and we will take corresponding actions after reviewing your request.