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Background  Cysteine, a sulfur-containing amino acid, plays an important role in a variety of cellular functions such as protein biosynthesis, methylation, and polyamine and glutathione syntheses. In trypanosomatids, glutathione is conjugated with spermidine to form the specific antioxidant thiol trypanothione (T[SH] 2 ) that plays a central role in maintaining intracellular redox homeostasis and providing defence against oxidative stress.    Methods  We cloned and characterised genes coding for a cystathionine β-synthase (CβS) and cysteine synthase (CS), key enzymes of the transsulfuration and assimilatory pathways, respectively, from the hemoflagellate protozoan parasite  Trypanosoma rangeli .    Results  Our results show that  T. rangeli  CβS (TrCβS), similar to its homologs in  T. cruzi , contains the catalytic domain essential for enzymatic activity. Unlike the enzymes in bacteria, plants, and other parasites,  T. rangeli  CS lacks two of the four lysine residues (Lys 26  and Lys 184 ) required for activity. Enzymatic studies using  T. rangeli  extracts confirmed the absence of CS activity but confirmed the expression of an active CβS. Moreover, CβS biochemical assays revealed that the  T. rangeli  CβS enzyme also has serine sulfhydrylase activity.    Conclusion  These findings demonstrate that the RTS pathway is active in  T. rangeli , suggesting that this may be the only pathway for cysteine biosynthesis in this parasite. In this sense, the RTS pathway appears to have an important functional role during the insect stage of the life cycle of this protozoan parasite.

Transsulfuration is an active pathway for cysteine biosynthesis in Trypanosoma rangeli