Permutation of the active site motif of tryparedoxin 2.

@article{Steinert2000PermutationOT,
  title={Permutation of the active site motif of tryparedoxin 2.},
  author={Peter Steinert and Karin Plank-Schumacher and M. Montemartini and Hans J{\"u}rgen Hecht and Leopold Floh{\'e}},
  journal={Biological chemistry},
  year={2000},
  volume={381 3},
  pages={211-9}
}
Tryparedoxins (TXN) are thioredoxin-related proteins which, as trypanothione:peroxiredoxin oxidoreductases, constitute the trypanothione-dependent antioxidant defense and may also serve as substrates for ribonucleotide reductase in trypanosomatids. The active site motif of TXN2, 40WCPPCR45, of Crithidia fasciculata was mutated by site-directed mutagenesis and eight corresponding muteins were expressed in E. coli as terminally His-tagged proteins, purified to homogeneity by nickel chelate… CONTINUE READING