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 Heilbronn, J.
Right arrow Articles by Berger, B. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Heilbronn, J.
Right arrow Articles by Berger, B. J.

 Previous Article  |  Next Article 

Journal of Bacteriology, March 1999, p. 1739-1747, Vol. 181, No. 6
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Tyrosine Aminotransferase Catalyzes the Final Step of Methionine Recycling in Klebsiella pneumoniae

Jacqueline Heilbronn,1,2 Judith Wilson,1 and Bradley J. Berger1,*

Department of Biochemistry, University of Dundee,1 and Scottish Crop Research Institute, Invergowrie,2 Dundee, United Kingdom

Received 8 September 1998/Accepted 12 January 1999

An aminotransferase which catalyzes the final step in methionine recycling from methylthioadenosine, the conversion of alpha -ketomethiobutyrate to methionine, has been purified from Klebsiella pneumoniae and characterized. The enzyme was found to be a homodimer of 45-kDa subunits, and it catalyzed methionine formation primarily using aromatic amino acids and glutamate as the amino donors. Histidine, leucine, asparagine, and arginine were also functional amino donors but to a lesser extent. The N-terminal amino acid sequence of the enzyme was determined and found to be almost identical to the N-terminal sequence of both the Escherichia coli and Salmonella typhimurium tyrosine aminotransferases (tyrB gene products). The structural gene for the tyrosine aminotransferase was cloned from K. pneumoniae and expressed in E. coli. The deduced amino acid sequence displayed 83, 80, 38, and 34% identity to the tyrosine aminotransferases from E. coli, S. typhimurium, Paracoccus denitrificans, and Rhizobium meliloti, respectively, but it showed less than 13% identity to any characterized eukaryotic tyrosine aminotransferase. Structural motifs around key invariant residues placed the K. pneumoniae enzyme within the Ia subfamily of aminotransferases. Kinetic analysis of the aminotransferase showed that reactions of an aromatic amino acid with alpha -ketomethiobutyrate and of glutamate with alpha -ketomethiobutyrate proceed as favorably as the well-known reactions of tyrosine with alpha -ketoglutarate and tyrosine with oxaloacetate normally associated with tyrosine aminotransferases. The aminotransferase was inhibited by the aminooxy compounds canaline and carboxymethoxylamine but not by substrate analogues, such as nitrotyrosine or nitrophenylalanine.

* Corresponding author. Mailing address: Div. of Molecular Parasitology & Biological Chemistry, Wellcome Trust Bldg., Dept. of Biochemistry, University of Dundee, Dundee, United Kingdom DD1 5EH. Phone: 44-(0)1382-345761. Fax: 44-(0)1382-345893. E-mail: bjberger{at}bad.dundee.ac.uk.

Journal of Bacteriology, March 1999, p. 1739-1747, Vol. 181, No. 6
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Lartey, F. M., Austic, R. E. (2009). Phenylalanine hydroxylase activity and expression in chicks subjected to phenylalanine imbalance or phenylalanine toxicity. Poult. Sci. 88: 774-783 [Abstract] [Full Text]  
  • Schuster, J., Knill, T., Reichelt, M., Gershenzon, J., Binder, S. (2006). BRANCHED-CHAIN AMINOTRANSFERASE4 Is Part of the Chain Elongation Pathway in the Biosynthesis of Methionine-Derived Glucosinolates in Arabidopsis. Plant Cell 18: 2664-2679 [Abstract] [Full Text]  
  • Carre-Mlouka, A., Mejean, A., Quillardet, P., Ashida, H., Saito, Y., Yokota, A., Callebaut, I., Sekowska, A., Dittmann, E., Bouchier, C., de Marsac, N. T. (2006). A New Rubisco-like Protein Coexists with a Photosynthetic Rubisco in the Planktonic Cyanobacteria Microcystis. J. Biol. Chem. 281: 24462-24471 [Abstract] [Full Text]  
  • Hosono, A., Mizuguchi, H., Hayashi, H., Goto, M., Miyahara, I., Hirotsu, K., Kagamiyama, H. (2003). Glutamine:phenylpyruvate Aminotransferase from an Extremely Thermophilic Bacterium, Thermus thermophilus HB8. J Biochem 134: 843-851 [Abstract] [Full Text]  
  • Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N., Yokota, A. (2003). A Functional Link Between RuBisCO-like Protein of Bacillus and Photosynthetic RuBisCO. Science 302: 286-290 [Abstract] [Full Text]  
  • Berger, B. J., English, S., Chan, G., Knodel, M. H. (2003). Methionine Regeneration and Aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis. J. Bacteriol. 185: 2418-2431 [Abstract] [Full Text]  
  • Berger, L. C., Wilson, J., Wood, P., Berger, B. J. (2001). Methionine Regeneration and Aspartate Aminotransferase in Parasitic Protozoa. J. Bacteriol. 183: 4421-4434 [Abstract] [Full Text]  
  • Berger, B. J. (2000). Antimalarial Activities of Aminooxy Compounds. Antimicrob. Agents Chemother. 44: 2540-2542 [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»