One of the major disadvantages of this approach is that the binding affinity of these competitive inhibitors must be very high because parasite survival is only compromised when the activity of this enzyme is reduced by more than 90%, which has turned out to be a very elusive goal in vivo. The majority of TryR enzyme inhibitors described in the literature interact at the active site where TS 2 binds. TryR is a validated therapeutic target for the discovery of antileishmanial drugs. ![]() The cellular role of TryR and T 2 is to maintain intracellular redox equilibrium, in a similar manner to that exerted by the glutathione-glutathione disulfide reductase pair in mammals. TryR catalyzes the NADPH-dependent reduction of trypanothione disulfide (TS 2) to the corresponding dithiol (T 2). ![]() ![]() Trypanothione disulfide reductase (TryR), an essential flavoprotein of Leishmania parasites, is a homodimeric enzyme crucial for antioxidant defense against trypanosomatids, and it is absent in humans.
0 Comments
Leave a Reply. |