This Article
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 Schrumpf, B
Right arrow Articles by Sahm, H
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schrumpf, B
Right arrow Articles by Sahm, H

 Previous Article  |  Next Article 

J Bacteriol. 1991 July; 173(14): 4510-4516

research-article

A functionally split pathway for lysine synthesis in Corynebacterium glutamicium.

B Schrumpf, A Schwarzer, J Kalinowski, A Pühler, L Eggeling and H Sahm

Institut für Biotechnologie, Jülich, Federal Republic of Germany.

ABSTRACT

Three different pathways of D,L-diaminopimelate and L-lysine synthesis are known in procaryotes. Determinations of the corresponding enzyme activities in Escherichia coli, Bacillus subtilis, and Bacillus sphaericus verified the fact that in each of these bacteria only one of the possible pathways operates. However, in Corynebacterium glutamicum activities are present which allow in principle the use of the dehydrogenase variant and succinylase variant of lysine synthesis together. Applying gene-directed mutagenesis, various C. glutamicum strains were constructed with interrupted ddh gene. These mutants have an inactive dehydrogenase pathway but are still prototrophic, which is proof that the succinylase pathway of D,L-diaminopimelate synthesis can be utilized. In strains with an increased flow of precursors to D,L-diaminopimelate, however, the inactivation of the dehydrogenase pathway resulted in a reduced formation of lysine, with concomitant accumulation of N-succinyl-diaminopimelate in the cytosol up to a concentration of 25 mM. These data show (i) that both pathways can operate in C. glutamicum for D,L-diaminopimelate and L-lysine synthesis, (ii) that the dehydrogenase pathway is not essential, and (iii) that the dehydrogenase pathway is a prerequisite for handling an increased flow of metabolites to D,L-diaminopimelate.

J Bacteriol. 1991 July; 173(14): 4510-4516




This article has been cited by other articles:

  • Blombach, B., Hans, S., Bathe, B., Eikmanns, B. J. (2009). Acetohydroxyacid Synthase, a Novel Target for Improvement of L-Lysine Production by Corynebacterium glutamicum. Appl. Environ. Microbiol. 75: 419-427 [Abstract] [Full Text]  
  • Hudson, A. O., Gilvarg, C., Leustek, T. (2008). Biochemical and Phylogenetic Characterization of a Novel Diaminopimelate Biosynthesis Pathway in Prokaryotes Identifies a Diverged Form of LL-Diaminopimelate Aminotransferase. J. Bacteriol. 190: 3256-3263 [Abstract] [Full Text]  
  • Seibold, G., Dempf, S., Schreiner, J., Eikmanns, B. J. (2007). Glycogen formation in Corynebacterium glutamicum and role of ADP-glucose pyrophosphorylase. Microbiology 153: 1275-1285 [Abstract] [Full Text]  
  • Schreiner, M. E., Riedel, C., Holatko, J., Patek, M., Eikmanns, B. J. (2006). Pyruvate:Quinone Oxidoreductase in Corynebacterium glutamicum: Molecular Analysis of the pqo Gene, Significance of the Enzyme, and Phylogenetic Aspects. J. Bacteriol. 188: 1341-1350 [Abstract] [Full Text]  
  • Silberbach, M., Schafer, M., Huser, A. T., Kalinowski, J., Puhler, A., Kramer, R., Burkovski, A. (2005). Adaptation of Corynebacterium glutamicum to Ammonium Limitation: a Global Analysis Using Transcriptome and Proteome Techniques. Appl. Environ. Microbiol. 71: 2391-2402 [Abstract] [Full Text]  
  • Netzer, R., Peters-Wendisch, P., Eggeling, L., Sahm, H. (2004). Cometabolism of a Nongrowth Substrate: L-Serine Utilization by Corynebacterium glutamicum. Appl. Environ. Microbiol. 70: 7148-7155 [Abstract] [Full Text]  
  • Hwang, B.-J., Yeom, H.-J., Kim, Y., Lee, H.-S. (2002). Corynebacterium glutamicum Utilizes both Transsulfuration and Direct Sulfhydrylation Pathways for Methionine Biosynthesis. J. Bacteriol. 184: 1277-1286 [Abstract] [Full Text]  
  • Molenaar, D., van der Rest, M. E., Drysch, A., Yücel, R. (2000). Functions of the Membrane-Associated and Cytoplasmic Malate Dehydrogenases in the Citric Acid Cycle of Corynebacterium glutamicum. J. Bacteriol. 182: 6884-6891 [Abstract] [Full Text]  
  • Fuchs, T. M., Schneider, B., Krumbach, K., Eggeling, L., Gross, R. (2000). Characterization of a Bordetella pertussis Diaminopimelate (DAP) Biosynthesis Locus Identifies dapC, a Novel Gene Coding for an N-Succinyl-L,L-DAP Aminotransferase. J. Bacteriol. 182: 3626-3631 [Abstract] [Full Text]  
  • Wendisch, V. F., de Graaf, A. A., Sahm, H., Eikmanns, B. J. (2000). Quantitative Determination of Metabolic Fluxes during Coutilization of Two Carbon Sources: Comparative Analyses with Corynebacterium glutamicum during Growth on Acetate and/or Glucose. J. Bacteriol. 182: 3088-3096 [Abstract] [Full Text]  
  • Hochuli, M., Patzelt, H., Oesterhelt, D., Wüthrich, K., Szyperski, T. (1999). Amino Acid Biosynthesis in the Halophilic Archaeon Haloarcula hispanica. J. Bacteriol. 181: 3226-3237 [Abstract] [Full Text]  
  • Wehrmann, A., Phillipp, B., Sahm, H., Eggeling, L. (1998). . J. Bacteriol. 180: 3159-3165 [Abstract]  
  • Siewe, R. M., Weil, B., Burkovski, A., Eikmanns, B. J., Eikmanns, M., Krämer, R. (1996). Functional and Genetic Characterization of the (Methyl)ammonium Uptake Carrier of Corynebacterium glutamicum. J. Biol. Chem. 271: 5398-5403 [Abstract] [Full Text]  
  • Petersen, S., de Graaf, A. A., Eggeling, L., Mollney, M., Wiechert, W., Sahm, H. (2000). In Vivo Quantification of Parallel and Bidirectional Fluxes in the Anaplerosis of Corynebacterium glutamicum. J. Biol. Chem. 275: 35932-35941 [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»