Pathway choice in glutamate synthesis in Escherichia coli

Journal of Bacteriology

Volumn 180, Issue 17, 1998, Pages 4571-4575

  Helling, Robert B ^a,b  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLUCOSE; GLUTAMATE AMMONIA LIGASE; GLUTAMATE SYNTHASE; GLUTAMIC ACID;

AMINO ACID SYNTHESIS; ARTICLE; BACTERIAL GROWTH; ENZYME ACTIVITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0031752273     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.17.4571-4575.1998     Document Type: Article

References (22)

1. Anderson, K. B., and K. von Meyenburg. 1980. Are growth rates of Escherichia coli limited by respiration? J. Bacteriol. 144:114-123.
2. Archer, C. D., X. Wang, and T. Elliott. 1993. Mutants defective in the energy-conserving NADH dehydrogenase of Salmonella typhimurium identified by a decrease in energy-dependent proteolysis after carbon starvation. Proc. Natl. Acad. Sci. USA 90:9877-9881.
3. Bender, R. A., K. A. Janssen, A. D. Resnick, M. Blumenberg, F. Foor, and B. Magasanik. 1977. Biochemical parameters of glutamine synthetase from Klebsiella aerogenes. J. Bacteriol. 129:1001-1009.
4. Goldman, B. S., K. K. Gabbert, and R. G. Kranz. 1996. The temperature-sensitive growth and survival phenotypes of Escherichia coli cydDC and cydAB are due to deficiencies in cytochrome bd and are corrected by exogenous catalase and reducing agents. J. Bacteriol. 178:6348-6351.
5. Guest, J. R. 1995. The Leeuwenhoek lecture, 1995. Adaptation to life without oxygen. Philos. Trans. R. Soc. Lond. B 350:189-202.
6. Helling, R. B. 1994. Why does Escherichia coli have two primary pathways for synthesis of glutamate? J. Bacteriol. 176:4664-4668.
7. Helling, R. B., T. Kinney, and J. Adams. 1981. The maintenance of plasmid-containing organisms in populations of Escherichia coli. J. Gen. Microbiol. 123:129-141.
8. Helling, R. B., C. N. Vargas, and J. Adams. 1987. Evolution of Escherichia coli during growth in a constant environment. Genetics 116:349-358.
9. Ikeda, T. P., A. E. Shauger, and S. Kustu. 1996. Salmonella typhimurium apparently perceives external nitrogen limitation as internal glutamine limitation. J. Mol. Biol. 259:589-607.
10. Jones, K. M., M. J. McPherson, A. J. Baron, I. W. Mattaj, C. L. Riodan, and J. C. Wooton. 1993. The gdhA1 point mutation in Escherichia coli CLR207 alters a key lysine residue of glutamate dehydrogenase. Mol. Gen. Genet. 240:286-289.
11. Kamberov, E. S., M. R. Atkinson, and A. J. Ninfa. 1995. The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP. J. Biol. Chem. 270:17797-17807.
12. + glutamate dehydrogenase in Escherichia coli. Curr. Microbiol. 28:63-65.
13. Magasanik, B. 1996. Regulation of nitrogen utilization, p. 1344-1356. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, D.C.
14. McGarvey, P., R. B. Helling, J.-Y. Lee, D. R. Engelke, and M. R. El-Gewely. 1988. Initiation of rrn transcription in chloroplasts of Euglena gracilis bacillaris. Curr. Genet. 14:493-500.
15. Miller, R. E., and E. R. Stadtman. 1972. Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein. J. Biol. Chem. 247:7407-7419.
16. Neijssel, O. M., and M. J. Teixeira de Mattos. 1994. The energetics of bacterial growth: a reassessment. Mol. Microbiol. 13:179-182.
17. Reitzer, L. J. 1996. Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine, and D-alanine, p. 391-407. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, D.C.
18. Sakamoto, N., A. M. Kotre, and M. A. Savageau. 1975. Glutamate dehydrogenase from Escherichia coli: purification and properties. J. Bacteriol. 124: 775-783.
19. + assimilation and osmoregulation in GOGAT (glutamate synthase)-deficient mutants of Escherichia coli. J. Bacteriol. 178:4105-4114.
20. Senior, P. J. 1975. Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: studies with the continuous-culture technique. J. Bacteriol. 123:407-418.
21. Siegele, D. A., K. R. C. Imlay, and J. A. Imlay. 1996. The stationary-phase-exit defect of cydC (surB) mutants is due to lack of a functional cytochrome oxidase. J. Bacteriol. 178:6091-6096.
22. Zambrano, M. M., and R. Kolter. 1993. Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase. J. Bacteriol. 175:5642-5647.