Mono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes.

ABSTRACT:

Significance

Glutaredoxins are ubiquitous small thiol proteins of the thioredoxin-fold superfamily. Two major groups are distinguished based on their active sites: the dithiol (2-C-Grxs) and the monothiol (1-C-Grxs) glutaredoxins with a CXXC and a CXXS active site motif, respectively. Glutaredoxins are involved in cellular redox and/or iron sulfur metabolism. Usually their functions are closely linked to the glutathione system. Trypanosomatids, the causative agents of several tropical diseases, rely on trypanothione as principal low molecular mass thiol, and their glutaredoxins readily react with the unique bis(glutathionyl) spermidine conjugate.

Recent advances

Two 2-C-Grxs and three 1-C-Grxs have been identified in pathogenic trypanosomatids. The 2-C-Grxs catalyze the redu

SUBMITTER: Comini MA 

PROVIDER: S-EPMC3739957 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature