Literature DB >> 10482536

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

D A Hogan1, T A Auchtung, R P Hausinger.   

Abstract

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.

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Year:  1999        PMID： 10482536      PMCID： PMC94115          DOI： 10.1128/JB.181.18.5876-5879.1999

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  8 in total

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Journal:  J Bacteriol       Date:  1999-03       Impact factor: 3.490

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Journal:  J Biol Chem       Date:  1993-11-15       Impact factor: 5.157

5.  Sulphonate utilization by enteric bacteria.

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Journal:  J Gen Microbiol       Date:  1993-02

6.  Comparative aspects of utilization of sulfonate and other sulfur sources by Escherichia coli K12.

Authors:  M R Uria-Nickelsen; E R Leadbetter; W Godchaux
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  8 in total
  18 in total

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10.  A suppressor of dioxygenase inhibition in a yeast model of SDH deficiency.

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