Tartrate-resistant phosphatase type 5 in Trypanosoma cruzi is important for resistance to oxidative stress promoted by hydrogen peroxide.

Trypanosoma cruzi (the causative agent of Chagas disease) presents a complex life cycle that involves adaptations in vertebrate and invertebrate hosts. As a protozoan parasite of hematophagous insects and mammalian hosts, T. cruzi is exposed to reactive oxygen species (ROS). To investigate the functionality of T. cruzi tartrate-resistant acid phosphatase type 5 (TcACP5), we cloned, superexpressed and purified the enzyme. Purified TcACP5 exhibited a V_max and apparent K_m for pNPP hydrolysis of 7.7 ± 0.2 nmol pNP × μg^-1 × h^-1 and 169.3 ± 22.6 μM, respectively. The pH dependence was characterized by sharp maximal activity at pH 5.0, and inhibition assays demonstrated its sensitivity to acid phosphatase inhibitors. Similar activities were obtained with saturating concentrations of P-Ser and P-Thr as substrates. The enzyme metabolizes hydrogen peroxide (H₂O₂) in vitro, and parasites superexpressing this enzyme were more resistant to oxidative stress promoted by H₂O₂. Taken together, these results suggest that TcACP5 plays a central role in phosphoryl transfer and redox reactions.