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Gene Review:

yedO - D-cysteine desulfhydrase

Escherichia coli CFT073

Nagasawa, T. et al., Riemenschneider, A. et al.

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Disease relevance of yedO

D-Cysteine desulfhydrase of Escherichia coli W3110 delta trpED102/F' delta trpED102 was physiologically characterized [1].

High impact information on yedO

No other activity of D-cysteine synthesis from O-acetyl-D-serine and sulfide was detected in a crude cell extract of E. coli which was immunotitrated with antibodies raised against the purified D-cysteine desulfhydrase [1].
Therefore, D-cysteine desulfhydrase does not contribute to 3-chloro-D-alanine detoxification in vivo [1].
Only D-cysteine but not L-cysteine was converted by D-CDes to pyruvate, H2S, and NH3 [2].
Western blot analysis of isolated organelles and localization studies using fusion constructs with the green fluorescent protein indicated an intracellular localization of the nuclear encoded D-CDes protein in the mitochondria [2].
Plants grown under low sulfate concentration showed an accumulation of D-CDes RNA and increased protein levels, the D-CDes activity was almost unchanged [2].

Chemical compound and disease context of yedO

Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1 [1].

Associations of yedO with chemical compounds

D-Cysteine desulfhydrase catalyzed not only the alpha, beta-elimination reaction of O-acetyl-D-serine to form pyruvate, acetic acid and ammonia, but also the beta-replacement reaction of O-acetyl-D-serine with sulfide to form D-cysteine [1].

References

Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1. Nagasawa, T., Ishii, T., Yamada, H. Arch. Microbiol. (1988) [Pubmed]
Isolation and characterization of a D-cysteine desulfhydrase protein from Arabidopsis thaliana. Riemenschneider, A., Wegele, R., Schmidt, A., Papenbrock, J. FEBS J. (2005) [Pubmed]

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