Skip to main content
NCBI home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1991 Jul;57(7):2012–2015. doi: 10.1128/aem.57.7.2012-2015.1991

Nutritional complementation of oxidative glucose metabolism in Escherichia coli via pyrroloquinoline quinone-dependent glucose dehydrogenase and the Entner-Doudoroff pathway.

M Adamowicz 1, T Conway 1, K W Nickerson 1
PMCID: PMC183513  PMID: 1654044

Abstract

Two glucose-negative Escherichia coli mutants (ZSC113 and DF214) were unable to grow on glucose as the sole carbon source unless supplemented with pyrroloquinoline quinone (PQQ). PQQ is the cofactor for the periplasmic enzyme glucose dehydrogenase, which converts glucose to gluconate. Aerobically, E. coli ZSC113 grew on glucose plus PQQ with a generation time of 65 min, a generation time about the same as that for wild-type E. coli in a defined glucose-salts medium. Thus, for E. coli ZSC113 the Enter-Doudoroff pathway was fully able to replace the Embden-Meyerhof-Parnas pathway. In the presence of 5% sodium dodecyl sulfate, PQQ no longer acted as a growth factor. Sodium dodecyl sulfate inhibited the formation of gluconate from glucose but not gluconate metabolism. Adaptation to PQQ-dependent growth exhibited long lag periods, except under low-phosphate conditions, in which the PhoE porin would be expressed. We suggest that E. coli has maintained the apoenzyme for glucose dehydrogenase and the Entner-Doudoroff pathway as adaptations to an aerobic, low-phosphate, and low-detergent aquatic environment.

Full text

PDF
2012

Selected References

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

  1. Adamowicz M., Kelley P. M., Nickerson K. W. Detergent (sodium dodecyl sulfate) shock proteins in Escherichia coli. J Bacteriol. 1991 Jan;173(1):229–233. doi: 10.1128/jb.173.1.229-233.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ameyama M., Matsushita K., Shinagawa E., Hayashi M., Adachi O. Pyrroloquinoline quinone: excretion by methylotrophs and growth stimulation for microorganisms. Biofactors. 1988 Jan;1(1):51–53. [PubMed] [Google Scholar]
  3. Cleton-Jansen A. M., Goosen N., Fayet O., van de Putte P. Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase. J Bacteriol. 1990 Nov;172(11):6308–6315. doi: 10.1128/jb.172.11.6308-6315.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Curtis S. J., Epstein W. Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase. J Bacteriol. 1975 Jun;122(3):1189–1199. doi: 10.1128/jb.122.3.1189-1199.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Eisenberg R. C., Dobrogosz W. J. Gluconate metabolism in Escherichia coli. J Bacteriol. 1967 Mar;93(3):941–949. doi: 10.1128/jb.93.3.941-949.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fraenkel D. G., Levisohn S. R. Glucose and gluconate metabolism in an Escherichia coli mutant lacking phosphoglucose isomerase. J Bacteriol. 1967 May;93(5):1571–1578. doi: 10.1128/jb.93.5.1571-1578.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Istúriz T., Palmero E., Vitelli-Flores J. Mutations affecting gluconate catabolism in Escherichia coli. Genetic mapping of the locus for the thermosensitive gluconokinase. J Gen Microbiol. 1986 Nov;132(11):3209–3219. doi: 10.1099/00221287-132-11-3209. [DOI] [PubMed] [Google Scholar]
  8. Kramer V. C., Calabrese D. M., Nickerson K. W. Growth of Enterobacter cloacae in the presence of 25% sodium dodecyl sulfate. Appl Environ Microbiol. 1980 Nov;40(5):973–976. doi: 10.1128/aem.40.5.973-976.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kramer V. C., Nickerson K. W. A transport-dependent energy burden imposed by growth of Enterobacter cloacae in the presence of 10% sodium dodecyl sulfate. Can J Microbiol. 1984 May;30(5):699–702. doi: 10.1139/m84-104. [DOI] [PubMed] [Google Scholar]
  10. Kramer V. C., Nickerson K. W., Hamlett N. V., O'Hara C. Prevalence of extreme detergent resistance among the Enterobacteriaceae. Can J Microbiol. 1984 May;30(5):711–713. doi: 10.1139/m84-106. [DOI] [PubMed] [Google Scholar]
  11. Kupor S. R., Fraenkel D. G. 6-phosphogluconolactonase mutants of Escherichia coli and a maltose blue gene. J Bacteriol. 1969 Dec;100(3):1296–1301. doi: 10.1128/jb.100.3.1296-1301.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Neu H. C., Heppel L. A. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Biol Chem. 1965 Sep;240(9):3685–3692. [PubMed] [Google Scholar]
  13. Roseman S., Meadow N. D. Signal transduction by the bacterial phosphotransferase system. Diauxie and the crr gene (J. Monod revisited). J Biol Chem. 1990 Feb 25;265(6):2993–2996. [PubMed] [Google Scholar]
  14. Schreyer R., Böck A. Phenotypic suppression of a fructose-1,6-diphosphate aldolase mutation in Escherichia coli. J Bacteriol. 1973 Jul;115(1):268–276. doi: 10.1128/jb.115.1.268-276.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Vinopal R. T., Hillman J. D., Schulman H., Reznikoff W. S., Fraenkel D. G. New phosphoglucose isomerase mutants of Escherichia coli. J Bacteriol. 1975 Jun;122(3):1172–1174. doi: 10.1128/jb.122.3.1172-1174.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Zablotny R., Fraenkel D. G. Glucose and gluconate metabolism in a mutant of Escherichia coli lacking gluconate-6-phosphate dehydrase. J Bacteriol. 1967 May;93(5):1579–1581. doi: 10.1128/jb.93.5.1579-1581.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. van Kleef M. A., Duine J. A. Factors relevant in bacterial pyrroloquinoline quinone production. Appl Environ Microbiol. 1989 May;55(5):1209–1213. doi: 10.1128/aem.55.5.1209-1213.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES