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. 1985 Sep;163(3):1109–1113. doi: 10.1128/jb.163.3.1109-1113.1985

Effect of some D-amino acids on the steady-state level of glutamine synthetase in Escherichia coli.

M A Berberich
PMCID: PMC219245  PMID: 2863253

Abstract

D-Glutamate can elicit an increase in the specific activity of glutamine synthetase (GS) when added to cells growing in the presence of high ammonia nitrogen. This effect is independent of glutamate dehydrogenase or glutamate synthase activities and could not be provoked by the addition of the various metabolites which participate in the regulation of GS in the covalent modification system. Neither could an increase in GS level be elicited by addition of any of the D-amino acids which function as allosteric effectors or inhibitors of GS activity. The increase in GS level could also be provoked by addition of D-lysine, D-threonine, or glycine to cells growing in an ammonia-rich medium. The increase in GS level generated by a mixture of D-glutamate, D-lysine, D-threonine, and glycine approximates the increase in GS level observed during step-down of a wild-type Escherichia coli culture from ammonia-sufficient to ammonia-limited growth conditions. Studies with mutants exhibiting alterations in GS regulation indicated that the increase elicited by the addition of D-amino acids depends on the presence of the wild-type glnD allele, although no direct correlation between a positive response and the state of adenylylation of GS can be made.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Berberich M. A. A glutamate-dependent phenotype in E. coli K12: the result of two mutations. Biochem Biophys Res Commun. 1972 Jun 28;47(6):1498–1503. doi: 10.1016/0006-291x(72)90242-2. [DOI] [PubMed] [Google Scholar]
  2. Chock P. B., Rhee S. G., Stadtman E. R. Interconvertible enzyme cascades in cellular regulation. Annu Rev Biochem. 1980;49:813–843. doi: 10.1146/annurev.bi.49.070180.004121. [DOI] [PubMed] [Google Scholar]
  3. Garcia E., Federici M., Rhee S. G., Berberich M. A. Glutamine synthetase cascade: enrichment of uridylyltransferase in Escherichia coli carrying hybrid ColE1 plasmids. Arch Biochem Biophys. 1980 Aug;203(1):181–189. doi: 10.1016/0003-9861(80)90167-8. [DOI] [PubMed] [Google Scholar]
  4. Ginsburg A. Conformational changes in glutamine synthetase from Escherichia coli. II. Some characteristics of the equilibrium binding of feedback inhibitors to the enzyme. Biochemistry. 1969 Apr;8(4):1726–1740. doi: 10.1021/bi00832a056. [DOI] [PubMed] [Google Scholar]
  5. Ginsburg A., Yeh J., Hennig S. B., Denton M. D. Some effects of adenylylation on the biosynthetic properties of the glutamine synthetase from Escherichia coli. Biochemistry. 1970 Feb 3;9(3):633–649. doi: 10.1021/bi00805a025. [DOI] [PubMed] [Google Scholar]
  6. Irr J. D. Control of nucleotide metabolism and ribosomal ribonucleic acid synthesis during nitrogen starvation of Escherichia coli. J Bacteriol. 1972 May;110(2):554–561. doi: 10.1128/jb.110.2.554-561.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. LICHTENSTEIN N., ROSS H. E., COHEN P. P. Effect of alpha-methylglutamic acid on the enzymatic synthesis and hydrolysis of glutamine. J Biol Chem. 1953 Mar;201(1):117–123. [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. Lazzarini R. A., Cashel M., Gallant J. On the regulation of guanosine tetraphosphate levels in stringent and relaxed strains of Escherichia coli. J Biol Chem. 1971 Jul 25;246(14):4381–4385. [PubMed] [Google Scholar]
  10. Leive L. Release of lipopolysaccharide by EDTA treatment of E. coli. Biochem Biophys Res Commun. 1965 Nov 22;21(4):290–296. doi: 10.1016/0006-291x(65)90191-9. [DOI] [PubMed] [Google Scholar]
  11. Magasanik B. Genetic control of nitrogen assimilation in bacteria. Annu Rev Genet. 1982;16:135–168. doi: 10.1146/annurev.ge.16.120182.001031. [DOI] [PubMed] [Google Scholar]
  12. Miller R. E., Stadtman E. R. Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein. J Biol Chem. 1972 Nov 25;247(22):7407–7419. [PubMed] [Google Scholar]
  13. Mura U., Chock P. B., Stadtman E. R. Allosteric regulation of the state of adenylylation of glutamine synthetase in permeabilized cell preparations of Escherichia coli. Studies of monocyclic and bicyclic interconvertible enzyme cascades, in situ. J Biol Chem. 1981 Dec 25;256(24):13022–13029. [PubMed] [Google Scholar]
  14. Prusiner S., Stadtman E. R. On the regulation of glutaminase in E. coli: metabolite control. Biochem Biophys Res Commun. 1971 Dec 17;45(6):1474–1481. doi: 10.1016/0006-291x(71)90186-0. [DOI] [PubMed] [Google Scholar]
  15. Senior P. J. Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: studies with the continuous-culture technique. J Bacteriol. 1975 Aug;123(2):407–418. doi: 10.1128/jb.123.2.407-418.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Stadtman E. R., Smyrniotis P. Z., Davis J. N., Wittenberger M. E. Enzymic procedures for determining the average state of adenylylation of Escherichia coli glutamine synthetase. Anal Biochem. 1979 May;95(1):275–285. doi: 10.1016/0003-2697(79)90217-3. [DOI] [PubMed] [Google Scholar]
  17. Stephens J. C., Artz S. W., Ames B. N. Guanosine 5'-diphosphate 3'-diphosphate (ppGpp): positive effector for histidine operon transcription and general signal for amino-acid deficiency. Proc Natl Acad Sci U S A. 1975 Nov;72(11):4389–4393. doi: 10.1073/pnas.72.11.4389. [DOI] [PMC free article] [PubMed] [Google Scholar]

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