Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1986 Jul;167(1):393–395. doi: 10.1128/jb.167.1.393-395.1986

Regulation of glycerol kinase by enzyme IIIGlc of the phosphoenolpyruvate:carbohydrate phosphotransferase system.

M de Boer, C P Broekhuizen, P W Postma
PMCID: PMC212891  PMID: 3013838

Abstract

Wild-type glycerol kinase of Escherichia coli is inhibited by both nonphosphorylated enzyme IIIGlc of the phosphoenolpyruvate:carbohydrate phosphotransferase system and fructose 1,6-diphosphate. Mutant glycerol kinase, resistant to inhibition by fructose 1,6-diphosphate, was much less sensitive to inhibition by enzyme IIIGlc. The difference between the wild-type and mutant enzymes was even greater when inhibition was measured in the presence of both enzyme IIIGlc and fructose 1,6-diphosphate. The binding of enzyme IIIGlc to glycerol kinase required the presence of the substrate glycerol.

Full text

PDF
393

Selected References

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

  1. Berman M., Lin E. C. Glycerol-specific revertants of a phosphoenolpyruvate phosphotransferase mutant: suppression by the desensitization of glycerol kinase to feedback inhibition. J Bacteriol. 1971 Jan;105(1):113–120. doi: 10.1128/jb.105.1.113-120.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Lengeler J. W., Mayer R. J., Schmid K. Phosphoenolpyruvate-dependent phosphotransferase system enzyme III and plasmid-encoded sucrose transport in Escherichia coli K-12. J Bacteriol. 1982 Jul;151(1):468–471. doi: 10.1128/jb.151.1.468-471.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Nelson S. O., Postma P. W. Interactions in vivo between IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system and the glycerol and maltose uptake systems of Salmonella typhimurium. Eur J Biochem. 1984 Feb 15;139(1):29–34. doi: 10.1111/j.1432-1033.1984.tb07971.x. [DOI] [PubMed] [Google Scholar]
  4. Nelson S. O., Schuitema A. R., Benne R., van der Ploeg L. H., Plijter J. S., Aan F., Postma P. W. Molecular cloning, sequencing, and expression of the crr gene: the structural gene for IIIGlc of the bacterial PEP:glucose phosphotransferase system. EMBO J. 1984 Jul;3(7):1587–1593. doi: 10.1002/j.1460-2075.1984.tb02015.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Nelson S. O., Wright J. K., Postma P. W. The mechanism of inducer exclusion. Direct interaction between purified III of the phosphoenolpyruvate:sugar phosphotransferase system and the lactose carrier of Escherichia coli. EMBO J. 1983;2(5):715–720. doi: 10.1002/j.1460-2075.1983.tb01490.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Novotny M. J., Frederickson W. L., Waygood E. B., Saier M. H., Jr Allosteric regulation of glycerol kinase by enzyme IIIglc of the phosphotransferase system in Escherichia coli and Salmonella typhimurium. J Bacteriol. 1985 May;162(2):810–816. doi: 10.1128/jb.162.2.810-816.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Postma P. W., Epstein W., Schuitema A. R., Nelson S. O. Interaction between IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system and glycerol kinase of Salmonella typhimurium. J Bacteriol. 1984 Apr;158(1):351–353. doi: 10.1128/jb.158.1.351-353.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Postma P. W., Lengeler J. W. Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria. Microbiol Rev. 1985 Sep;49(3):232–269. doi: 10.1128/mr.49.3.232-269.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Scholte B. J., Postma P. W. Competition between two pathways for sugar uptake by the phosphoenolpyruvate-dependent sugar phosphotransferase system in Salmonella typhimurium. Eur J Biochem. 1981;114(1):51–58. doi: 10.1111/j.1432-1033.1981.tb06171.x. [DOI] [PubMed] [Google Scholar]
  10. Scholte B. J., Schuitema A. R., Postma P. W. Isolation of IIIGlc of the phosphoenolpyruvate-dependent glucose phosphotransferase system of Salmonella typhimurium. J Bacteriol. 1981 Oct;148(1):257–264. doi: 10.1128/jb.148.1.257-264.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Thorner J. W., Paulus H. Catalytic and allosteric properties of glycerol kinase from Escherichia coli. J Biol Chem. 1973 Jun 10;248(11):3922–3932. [PubMed] [Google Scholar]
  12. Thorner J. W., Paulus H. Composition and subunit structure of glycerol kinase from Escherichia coli. J Biol Chem. 1971 Jun 25;246(12):3885–3894. [PubMed] [Google Scholar]

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

RESOURCES