Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168.

@article{Dorenbos2002ThioldisulfideOA,
  title={Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168.},
  author={Ronald Dorenbos and Torsten Stein and Jorrit Kabel and Claude Bruand and Albert Bolhuis and Sierd Bron and Wim J Quax and Jan Maarten van Dijl},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 19},
  pages={16682-8}
}
Thiol-disulfide oxidoreductases are required for disulfide bond formation in proteins that are exported from the cytoplasm. Four enzymes of this type, termed BdbA, BdbB, BdbC, and BdbD, have been identified in the Gram-positive eubacterium Bacillus subtilis. BdbC and BdbD have been shown to be critical for the folding of a protein required for DNA uptake during natural competence. In contrast, no function has been assigned so far to the BdbA and BdbB proteins. The bdbA and bdbB genes are… CONTINUE READING

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