Cloning and characterization of a sulfonate/alpha-ketoglutarate dioxygenase from Saccharomyces cerevisiae

J Bacteriol. 1999 Sep;181(18):5876-9. doi: 10.1128/JB.181.18.5876-5879.1999.


The Saccharomyces cerevisiae open reading frame YLL057c is predicted to encode a gene product with 31.5% amino acid sequence identity to Escherichia coli taurine/alpha-ketoglutarate dioxygenase and 27% identity to Ralstonia eutropha TfdA, a herbicide-degrading enzyme. Purified recombinant yeast protein is shown to be an Fe(II)-dependent sulfonate/alpha-ketoglutarate dioxygenase. Although taurine is a poor substrate, a variety of other sulfonates are utilized, with the best natural substrates being isethionate and taurocholate. Disruption of the gene encoding this enzyme negatively affects the use of isethionate and taurine as sulfur sources by S. cerevisiae, providing strong evidence that YLL057c plays a role in sulfonate catabolism.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Chromosomes, Fungal / genetics
  • Cloning, Molecular
  • Cupriavidus necator / genetics
  • Dioxygenases
  • Escherichia coli / genetics
  • Kinetics
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / isolation & purification
  • Mixed Function Oxygenases / metabolism*
  • Mutagenesis
  • Open Reading Frames
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins*
  • Sequence Deletion
  • Substrate Specificity


  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Mixed Function Oxygenases
  • Dioxygenases
  • JLP1 protein, S cerevisiae