Identification of a novel, thiol-containing co-factor essential for glutathione reductase enzyme activity in trypanosomatids.
Soluble extracts of Trypanosoma brucei, T. cruzi, Leishmania mexicana and Crithidia fasciculata contain a novel enzyme capable of reducing oxidized glutathione by NADPH solely in the presence of an unidentified, dialyzable, heat stable co-factor. Evidence is presented showing that co-factor contains enzymatically reducible thiol group(s), essential for activity. The co-factor is possibly unique to the Kinetoplastida, since dialysate extracts from a wide selection of other organisms would not substitute for trypanosomatid co-factor preparations.
D000818:Animals; D003421:Crithidia / Q000201:enzymology; D056890:Eukaryota / Q000201:enzymology*; D005978:Glutathione / Q000378:metabolism; D005980:Glutathione Reductase / Q000378:metabolism; D007891:Leishmania / Q000201:enzymology; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D013438:Sulfhydryl Compounds / Q000502:physiology; D014345:Trypanosoma / Q000201:enzymology
D013438:Sulfhydryl Compounds; D009249:NADP; D005980:Glutathione Reductase; D005978:Glutathione