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Background  The glyoxalase pathway, which includes two enzymes, glyoxalase 1 and 2 (Glo1 and Glo2), is a ubiquitous cellular system responsible for the removal of cytotoxic methylglyoxal produced during glycolysis. Protozoan parasites, including  Toxoplasma gondii  ( T. gondii ) tachyzoites, produce methylglyoxal because of increased glycolytic fluxes. A Glo1 inhibitor such as curcumin could be considered a drug candidate for anti-protozoan, anti-inflammatory, and anti-cancer therapy.    Methods  The  T. gondii  Glo1 gene (TgGlo1) was cloned and the recombinant protein was produced. Enzyme kinetics of TgGlo1 and five mutants were evaluated by adding methylglyoxal and glutathione to a reaction mixture. Finally, the inhibitory effects of various concentrations of curcumin on recombinant TgGlo1 were evaluated using in vitro cultures of  T. gondii .    Results  Active recombinant TgGlo1 was successfully produced and the active sites (E166 and E251) of TgGlo1 were verified by point mutagenesis. Curcumin at the tested doses inhibited the enzymatic activity of recombinant TgGlo1 as well as the parasitic propagation of in vitro-cultured  T. gondii . The K i  and IC 50  were 12.9 ± 0.5 μM and 38.3 ± 0.9 μM, respectively.    Conclusion  The inhibitory effect of curcumin on the enzymatic activity of TgGlo1 and parasitic propagation of  T. gondii  could be explored in the potential development of a potent drug for the treatment of toxoplasmosis. However, considering the fact that curcumin is known to have many effects on other molecules in the micromolar range, further elucidation of curcumin’s direct inhibition of the glyoxalase system of  T. gondii  will be needed.    Electronic supplementary material  The online version of this article (doi:10.1186/s13071-015-1268-5) contains supplementary material, which is available to authorized users.

Characterization of Toxoplasma gondii glyoxalase 1 and evaluation of inhibitory effects of curcumin on the enzyme and parasite cultures