This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hogan, D. A.
Right arrow Articles by Hausinger, R. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hogan, D. A.
Right arrow Articles by Hausinger, R. P.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 1999, p. 5876-5879, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Cloning and Characterization of a Sulfonate/alpha -Ketoglutarate Dioxygenase from Saccharomyces cerevisiae

Deborah A. Hogan,1,2 Thomas A. Auchtung,2 and Robert P. Hausinger1,2,3,*

Center for Microbial Ecology1 and Departments of Microbiology2 and Biochemistry,3 Michigan State University, East Lansing, Michigan 48824

Received 19 February 1999/Accepted 13 July 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.

* Corresponding author. Mailing address: Department of Microbiology, 160 Giltner Hall, Michigan State University, East Lansing, MI 48824. Phone: (517) 353-9675. Fax: (517) 353-8957. E-mail: hausinge{at}pilot.msu.edu.

Journal of Bacteriology, September 1999, p. 5876-5879, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Smith, E. H., Janknecht, R., Maher, L. J. III (2007). Succinate inhibition of {alpha}-ketoglutarate-dependent enzymes in a yeast model of paraganglioma. Hum Mol Genet 16: 3136-3148 [Abstract] [Full Text]  
  • Clifton, I. J., Doan, L. X., Sleeman, M. C., Topf, M., Suzuki, H., Wilmouth, R. C., Schofield, C. J. (2003). Crystal Structure of Carbapenem Synthase (CarC). J. Biol. Chem. 278: 20843-20850 [Abstract] [Full Text]  
  • Ryle, M. J., Koehntop, K. D., Liu, A., Que, L. Jr., Hausinger, R. P. (2003). Bioinorganic Chemistry Special Feature: Interconversion of two oxidized forms of taurine/alpha -ketoglutarate dioxygenase, a non-heme iron hydroxylase: Evidence for bicarbonate binding. Proc. Natl. Acad. Sci. USA 100: 3790-3795 [Abstract] [Full Text]  
  • White, A. K., Metcalf, W. W. (2002). Isolation and Biochemical Characterization of Hypophosphite/ 2-Oxoglutarate Dioxygenase. A NOVEL PHOSPHORUS-OXIDIZING ENZYME FROM PSEUDOMONAS STUTZERI WM88. J. Biol. Chem. 277: 38262-38271 [Abstract] [Full Text]  
  • Hogan, D. A., Smith, S. R., Saari, E. A., McCracken, J., Hausinger, R. P. (2000). Site-directed Mutagenesis of 2,4-Dichlorophenoxyacetic Acid/alpha -Ketoglutarate Dioxygenase. IDENTIFICATION OF RESIDUES INVOLVED IN METALLOCENTER FORMATION AND SUBSTRATE BINDING. J. Biol. Chem. 275: 12400-12409 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»