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Updated: Jul 11, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
Glutathione transferases from parasites: a biochemical view
Anayetzin Torres-Rivera1, Abraham Landa
1Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México, Edificio A, 2o Piso, Ciudad Universitaria, México D.F. 04510, Mexico.
Abstract:
The glutathione transferase (GST) system of parasites represents the main detoxification mechanism of hydrophobic and electrophilic compounds. Parasites lack the CYP450 activity, hence part of its function has been taken over by other enzymes including GSTs. Cytosolic GSTs (cGSTs) are found in this system and constitute a versatile and numerous group that in parasites display many peculiarities in contrast to mammalian cGSTs. This review summarizes aspects of the biochemistry of parasite cGSTs such as substrate specificities, inhibitor sensitivities, classification, kinetics and catalysis, as well as some aspects of their protective role.
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