Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to D-cysteine.

@article{Soutourina2001RoleOD,
  title={Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to D-cysteine.},
  author={Julie Soutourina and Sylvain Blanquet and Pierre Plateau},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 44},
  pages={40864-72}
}
D-cysteine, a powerful inhibitor of Escherichia coli growth, is decomposed in vitro into pyruvate, H2S, and NH3 by D-cysteine desulfhydrase. To assess the role of this reaction in the adaptation of the bacterium to growth on D-cysteine, the gene of the desulfhydrase was cloned. It corresponds to the open reading frame yedO at 43.03 min on the genetic map of E. coli. The amino acid sequence deduced from this gene is homologous to those of several 1-aminocyclopropane-carboxylate deaminases… CONTINUE READING

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