title: Glutathione transferases from parasites: a biochemical view.
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.
authors: Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México, Edificio A, 2o Piso, Ciudad Universitaria, México D.F. 04510, Mexico.
authors: Anayetzin
authors: A
authors: Torres-Rivera
authors: Abraham
authors: A
authors: Landa
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D010271:Parasites / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D004791:Enzyme Inhibitors; D005982:Glutathione Transferase