• Title of article

    Glutathione transferases from parasites: A biochemical view

  • Author/Authors

    Anayetzin Torres-Rivera، نويسنده , , Abraham Landa، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2008
  • Pages
    14
  • From page
    99
  • To page
    112
  • 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.
  • Keywords
    Substrate specificity , GST , Kinetics , Parasites , crystals , Drug-design
  • Journal title
    Acta Tropica
  • Serial Year
    2008
  • Journal title
    Acta Tropica
  • Record number

    778571