Skip to main content
NCBI home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1985 Mar;49(3):505–508. doi: 10.1128/aem.49.3.505-508.1985

Effect of pH, temperature, and potassium sorbate on amino acid uptake in Salmonella typhimurium 7136.

E U Tuncan, S E Martin
PMCID: PMC373539  PMID: 3888108

Abstract

The effect of sorbate on L-serine and L-histidine uptake in Salmonella typhimurium was studied at various pH levels, temperatures, and amino acid and sorbate concentrations. Low pH had an apparent synergistic effect on amino acid uptake inhibition caused by sorbate. The relationship between sorbate concentration and the amount of amino acid uptake inhibition was not linear. Compared with L-histidine, L-serine uptake was more sensitive to changes in pH, temperature, and sorbate concentration. Various degrees of amino acid uptake inhibition by sorbate may be related to differences between amino acid transport systems. The results of this study suggest that sorbate acts as a noncompetitive inhibitor of amino acid uptake in S. typhimurium.

Full text

PDF
505

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. Ames G. F., Roth J. R. Histidine and aromatic permeases of Salmonella typhimurim. J Bacteriol. 1968 Nov;96(5):1742–1749. doi: 10.1128/jb.96.5.1742-1749.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ames G. F. Two methods for the assay of amino acid transport in bacteria. Methods Enzymol. 1974;32:843–849. doi: 10.1016/0076-6879(74)32085-x. [DOI] [PubMed] [Google Scholar]
  4. Berger E. A., Heppel L. A. Different mechanisms of energy coupling for the shock-sensitive and shock-resistant amino acid permeases of Escherichia coli. J Biol Chem. 1974 Dec 25;249(24):7747–7755. [PubMed] [Google Scholar]
  5. Boyaval P., Moreira E., Desmazeaud M. J. Transport of aromatic amino acids by Brevibacterium linens. J Bacteriol. 1983 Sep;155(3):1123–1129. doi: 10.1128/jb.155.3.1123-1129.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Devés R., Krupka R. M. A new approach in the kinetics of biological transport. The potential of reversible inhibition studies. Biochim Biophys Acta. 1978 Jun 16;510(1):186–200. doi: 10.1016/0005-2736(78)90140-2. [DOI] [PubMed] [Google Scholar]
  7. Eklund T. Inhibition of growth and uptake processes in bacteria by some chemical food preservatives. J Appl Bacteriol. 1980 Jun;48(3):423–432. doi: 10.1111/j.1365-2672.1980.tb01031.x. [DOI] [PubMed] [Google Scholar]
  8. Freese E., Sheu C. W., Galliers E. Function of lipophilic acids as antimicrobial food additives. Nature. 1973 Feb 2;241(5388):321–325. doi: 10.1038/241321a0. [DOI] [PubMed] [Google Scholar]
  9. Hong J. S., Hunt A. G., Masters P. S., Lieberman M. A. Requirements of acetyl phosphate for the binding protein-dependent transport systems in Escherichia coli. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1213–1217. doi: 10.1073/pnas.76.3.1213. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Krupka R. M. The kinetics of transport inhibition by noncompetitive inhibitors. J Membr Biol. 1983;74(3):175–182. doi: 10.1007/BF02332121. [DOI] [PubMed] [Google Scholar]
  11. Neal J. L. Analysis of Michaelis kinetics for two independent, saturable membrane transport functions. J Theor Biol. 1972 Apr;35(1):113–118. doi: 10.1016/0022-5193(72)90196-8. [DOI] [PubMed] [Google Scholar]
  12. Rosen B. P., Vasington F. D. Purification and characterization of a histidine-binding protein from Salmonella typhimurium LT-2 and its relationship to the histidine permease system. J Biol Chem. 1971 Sep 10;246(17):5351–5360. [PubMed] [Google Scholar]
  13. Sheu C. W., Salomon D., Simmons J. L., Sreevalsan T., Freese E. Inhibitory effects of lipophilic acids and related compounds on bacteria and mammalian cells. Antimicrob Agents Chemother. 1975 Mar;7(3):349–363. doi: 10.1128/aac.7.3.349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES