These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [2 phosphotransferase systems that control the second stage of phosphoenolpyruvate-dependent glucose phosphorylation in E. coli].
    Author: Golub EI, Garaev MM.
    Journal: Biokhimiia; 1975; 40(1):25-31. PubMed ID: 1095077.
    Abstract:
    Analysis of E. coli W mutants defective in glucose transport suggests an existence of two enzyme systems which carry out the second step of phosphoenolpyruvate (PEP)-dependent glucose phosphorylation, thus controlling the glucose transport into E. coli cells. One system (PTS-glu-alpha) controls phosphorylation and transport of both glucose and alpha-methylglucoside, the other system (PTS-glu-beta) controls phosphorylation and transport of glucose only. PTS-glu-alpha system is damaged in the mutants studied, but PTS-glu-beta system is intact. On account of this fact the mutants do not uptake 14-C-alpha-methylglucoside and their extracts are practically incapable of its phosphorylation, phosphoenolpyruvate being used as phosphate donor. At the same time the mutants are capable of 14-C-glucose uptake and PEP-dependent 14-C-glucose phosphorylation. In one of the strain, having the intact PTS-glu-alpha system, the uptake of glucose and alpha-methylglucoside was stimulated by the addiction of glucose in the cultural medium. No such effect was observed in bacteria with the disturbed PTS-glu-alpha system and the intact PTS-glu-beta system. Probably, the PTS-glu-alpha system can be inducible, in contrast with the PTS-glu-beta system. The damage of the PTS-glu-alpha system results in resistance of bacteria to glucose-induced inhibition of the enzyme synthesis.
    [Abstract] [Full Text] [Related] [New Search]