Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1965 Nov;90(5):1288–1295. doi: 10.1128/jb.90.5.1288-1295.1965

Glutamate Transport in Wild-Type and Mutant Strains of Escherichia coli

Yeheskel S Halpern 1, Meir Lupo 1
PMCID: PMC315815  PMID: 5321483

Abstract

Halpern, Yeheskel S. (Hebrew University-Hadassah Medical School, Jerusalem, Israel), and Meir Lupo. Glutamate transport in wild-type and mutant strains of Escherichia coli. J. Bacteriol. 90:1288–1295. 1965.—Mutants of Escherichia coli able to grow on glutamate as their source of carbon showed glutamate dehydrogenase and glutamate-oxaloacetate transaminase activities similar to those possessed by the parent strain. The mutants took up glutamate at a much faster rate and showed a several-fold greater capacity for concentrating the amino acid than did the corresponding parent strains. Curvilinear double reciprocal plots of velocity of uptake versus glutamate concentration were obtained with the E. coli H strains. A break in the curve of glutamate uptake was observed with the E. coli K-12 strains when incubated in a glucose medium. It is suggested that these findings may be due to allosteric activation of glutamate permease by its substrate.

Full text

PDF

Selected References

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

  1. AMES G. F. UPTAKE OF AMINO ACIDS BY SALMONELLA TYPHIMURIUM. Arch Biochem Biophys. 1964 Jan;104:1–18. doi: 10.1016/s0003-9861(64)80028-x. [DOI] [PubMed] [Google Scholar]
  2. AYENGAR P., ROBERTS E. Inhibition of utilization of glutamic acid by Lactobacillus arabinosus. Proc Soc Exp Biol Med. 1952 Mar;79(3):476–481. doi: 10.3181/00379727-79-19417. [DOI] [PubMed] [Google Scholar]
  3. DAVIS B. D., MINGIOLI E. S. Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol. 1950 Jul;60(1):17–28. doi: 10.1128/jb.60.1.17-28.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. FRIEDEN C. Glutamic dehydrogenase. I. The effect of coenzyme on the sedimentation velocity and kinetic behavior. J Biol Chem. 1959 Apr;234(4):809–814. [PubMed] [Google Scholar]
  5. HALPERN Y. S., UMBARGER H. E. Conversion of ammonia to amino groups in Escherichia coli. J Bacteriol. 1960 Sep;80:285–288. doi: 10.1128/jb.80.3.285-288.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. HALPERN Y. S., UMBARGER H. E. Utilization of L-glutamic and 2-oxoglutaric acid as sole sources of carbon by Escherichia coli. J Gen Microbiol. 1961 Oct;26:175–183. doi: 10.1099/00221287-26-2-175. [DOI] [PubMed] [Google Scholar]
  7. KESSEL D., LUBIN M. STABILITY OF ALPHA-HYDROGEN OF AMINO ACIDS DURING ACTIVE TRANSPORT. Biochemistry. 1965 Mar;4:561–565. doi: 10.1021/bi00879a029. [DOI] [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. MONOD J., CHANGEUX J. P., JACOB F. Allosteric proteins and cellular control systems. J Mol Biol. 1963 Apr;6:306–329. doi: 10.1016/s0022-2836(63)80091-1. [DOI] [PubMed] [Google Scholar]
  10. SANWAL B. D. Diphosphopyridine nucleotide and triphosphopyridine nucleotide linked glutamic dehydrogenases of Fusarium. Arch Biochem Biophys. 1961 May;93:377–386. doi: 10.1016/0003-9861(61)90281-8. [DOI] [PubMed] [Google Scholar]
  11. SANWAL B. D., LATA M. Effect of glutamic acid on the formation of two glutamic acid dehydrogenases of Neurospora. Biochem Biophys Res Commun. 1962 Jan 24;6:404–409. doi: 10.1016/0006-291x(62)90364-9. [DOI] [PubMed] [Google Scholar]
  12. SANWAL B. D., LATA M. The occurrence of two different glutamic dehydrogenases in Neurospora. Can J Microbiol. 1961 Jun;7:319–328. doi: 10.1139/m61-039. [DOI] [PubMed] [Google Scholar]
  13. SANWAL B. D., STACHOW C. S., COOK R. A. A KINETIC MODEL FOR THE MECHANISM OF ALLOSTERIC ACTIVATION OF NICOTINAMIDE-ADENINE DINUCLEOTIDE-SPECIFIC ISOCRITIC DEHYDROGENASE. Biochemistry. 1965 Mar;4:410–421. doi: 10.1021/bi00879a006. [DOI] [PubMed] [Google Scholar]
  14. SCRUTTON M. C., KEECH D. B., UTTER M. F. PYRUVATE CARBOXYLASE. IV. PARTIAL REACTIONS AND THE LOCUS OF ACTIVATION BY ACETYL COENZYME A. J Biol Chem. 1965 Feb;240:574–581. [PubMed] [Google Scholar]
  15. VENDER J., RICKENBERG H. V. AMMONIA METABOLISM IN A MUTANT OF ESCHERICHIA COLI LACKING GLUTAMATE DEHYDROGENASE. Biochim Biophys Acta. 1964 Jul 15;90:218–220. doi: 10.1016/0304-4165(64)90149-7. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES