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

Properties of a D-Glutamic Acid-Requiring Mutant of Escherichia coli

^a Laboratory for Microbiology, State University, Catharijnesingel 59, Utrecht, The Netherlands; and Institute of Genetics, University of Amsterdam, Amsterdam, The Netherlands

ABSTRACT

Some properties of a D-glutamic acid auxotroph of Escherichia coli B were studied. The mutant cells lysed in the absence of D-glutamic acid. Murein synthesis was impaired, accompanied by accumulation of uridine-5'-diphosphate-N-acetyl-muramyl-L-alanine (UDP-MurNac-L-Ala), as was shown by incubation of the mutant cells in a cell wall medium containing L-[¹⁴C]alanine. After incubation of the parental strain in a cell wall medium containing L-[¹⁴C]glutamic acid, the acid-precipitable radioactivity was lysozyme degradable to a large extent. Radioactive UDP-MurNac-pentapeptide was isolated from the L-[¹⁴C]glutamic acid-labeled parental cells. After hydrolysis, the label was exclusively present in glutamic acid, the majority of which had the stereo-isomeric D-configuration. Compared to the parent the mutant incorporated less L-[¹⁴C]glutamic acid from the wall medium into acid-precipitable material. Lysozyme degraded a smaller percentage of the acid-precipitable material of the mutant than of that of the parent. No radioactive uridine nucleotide precursors could be isolated from the mutant under these conditions. Attempts to identify the enzymatic defect in this mutant were not successful. The activity of UDP-MurNac-L-Ala:D-glutamic acid ligase (ADP; EC 6.3.2.9) (D-glutamic acid adding enzyme) is not affected by the mutation. Possible pathways for D-glutamic acid biosynthesis in E. coli B are discussed.

¹ Present address: University of Connecticut Health Center, Department of Microbiology, Farmington, Conn. 06032.

This article has been cited by other articles:

• Chatterjee, I., Somerville, G. A., Heilmann, C., Sahl, H.-G., Maurer, H. H., Herrmann, M. (2006). Very Low Ethanol Concentrations Affect the Viability and Growth Recovery in Post-Stationary-Phase Staphylococcus aureus Populations. Appl. Environ. Microbiol. 72: 2627-2636 [Abstract] [Full Text]  
• Lee, S.-G., Hong, S.-P., Song, J. J., Kim, S.-J., Kwak, M.-S., Sung, M.-H. (2006). Functional and Structural Characterization of Thermostable D-Amino Acid Aminotransferases from Geobacillus spp.. Appl. Environ. Microbiol. 72: 1588-1594 [Abstract] [Full Text]  
• Nishizawa, T., Asayama, M., Shirai, M. (2001). Cyclic heptapeptide microcystin biosynthesis requires the glutamate racemase gene. Microbiology 147: 1235-1241 [Abstract] [Full Text]  
• Berlyn, M. K. B. (1998). Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map. Microbiol. Mol. Biol. Rev. 62: 814-984 [Abstract] [Full Text]  
• Fotheringham, I. G., Bledig, S. A., Taylor, P. P. (1998). Characterization of the Genes Encoding D-Amino Acid Transaminase and Glutamate Racemase, Two D-Glutamate Biosynthetic Enzymes of Bacillus sphaericus ATCC 10208. J. Bacteriol. 180: 4319-4323 [Abstract] [Full Text]