Jul 21, 2006

Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteria

Journal of Bacteriology
John E DominyMartha H Stipanuk

Abstract

In metazoa and fungi, the catabolic dissimilation of cysteine begins with its sulfoxidation to cysteine sulfinic acid by the enzyme cysteine dioxygenase (CDO). In these organisms, CDO plays an important role in the homeostatic regulation of steady-state cysteine levels and provides important oxidized metabolites of cysteine such as sulfate and taurine. To date, there has been no experimental evidence for the presence of CDO in prokaryotes. Using PSI-BLAST searches and crystallographic information about the active-site geometry of mammalian CDOs, we identified a total of four proteins from Bacillus subtilis, Bacillus cereus, and Streptomyces coelicolor A3(2) that shared low overall identity to CDO (13 to 21%) but nevertheless conserved important active-site residues. These four proteins were heterologously expressed and purified to homogeneity by a single-step immobilized metal affinity chromatography procedure. The ability of these proteins to oxidize cysteine to cysteine sulfinic acid was then compared against recombinant rat CDO. The kinetic data strongly indicate that these proteins are indeed bona fide CDOs. Phylogenetic analyses of putative bacterial CDO homologs also indicate that CDO is distributed among species within t...Continue Reading

  • References23
  • Citations46

References

Mentioned in this Paper

Cysteine dioxygenase
Biochemical Pathway
Streptomyces coelicolor
Cysteine sulfinic acid
Catabolic Process
Oxidation
Taurine
Dioxygenases
Bacillus subtilis
Cysteine

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