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Gene Review:

dcyD - D-cysteine desulfhydrase, PLP-dependent

Escherichia coli str. K-12 substr. MG1655

Soutourina, J. et al., Nagasawa, T. et al.

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Disease relevance of dcyD

Finally, in the presence of the intact yedO gene, E. coli growth was improved by addition of D-cysteine as the sole sulfur source [1].

High impact information on dcyD

In agreement with a role of the desulfhydrase in sulfur metabolism, yedO expression was induced under conditions of sulfate limitation [1].
It corresponds to the open reading frame yedO at 43.03 min on the genetic map of E. coli [1].
D-cysteine, a powerful inhibitor of Escherichia coli growth, is decomposed in vitro into pyruvate, H2S, and NH3 by D-cysteine desulfhydrase [1].
D-Cysteine desulfhydrase also catalyzes the beta-replacement reaction of the chlorine of 3-chloro-D-alanine with thioglycolic acid to yield S-carboxymethyl-D-cysteine [2].

References

Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to D-cysteine. Soutourina, J., Blanquet, S., Plateau, P. J. Biol. Chem. (2001) [Pubmed]
D-Cysteine desulfhydrase of Escherichia coli. Purification and characterization. Nagasawa, T., Ishii, T., Kumagai, H., Yamada, H. Eur. J. Biochem. (1985) [Pubmed]

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