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Background The glyoxalase system is the main catabolic pathway of methylglyoxal, a toxic 2-oxoaldehyde which occurs in all living cells as a by-product of glycolysis [1,2]. Trypanosomatids, such as Leishmania infantum, are pathogenic microbial parasites which have glycolytic enzymes located in a specific cell organelle, the glycosome [3]. In these organisms, the usual glyoxalase cofactor glutathione is functionally replaced by trypanothione [4,5]. Inhibition of the glyoxalase pathway might cause the accumulation of methylglyoxal in the glycosome, hampering glycolysis and killing the parasite.

Potential role of the glyoxalase pathway as a drug target in Leishmania infantum: an exact steady-state model analysis