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  • Phosphotransferase system  (2)
  • HPr  (1)
  • [abr] NMR; nuclear magnetic resonance  (1)
  • [abr] amu; atomic mass units  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Journal of Molecular Biology 236 (1994), S. 1341-1355 
    ISSN: 0022-2836
    Schlagwort(e): HPr ; PTS ; X-ray structure ; [abr] ES-MS; electrospray mass spectroscopy ; [abr] HPr; histidine-containing protein ; [abr] MIR; multiple isomorphous replacement ; [abr] NMR; nuclear magnetic resonance ; [abr] P-HPr; Hisl5-phosphorylated HPr ; [abr] PTS; phosphoenolpyruvate ; [abr] SIR; single isomorphous replacement ; [abr] amu; atomic mass units ; [abr] r.m.s.; root-means-quare ; [abr] sugar phosphotransferase system ; crystallography ; phosphotransfer
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 250 (1996), S. 375-379 
    ISSN: 1617-4623
    Schlagwort(e): Key words Glucose transporter ; Phosphotransferase system ; Membrane proteins ; glcA/B ; Staphylococcus carnosus
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract  Phosphoenolpyruvate (PEP)-dependent phosphorylation experiments have indicated that the gram-positive bacterium Staphylococcus carnosus possesses an EIICBA fusion protein specific for glucose. Here we report the cloning of a 7 kb genomic DNA fragment containing two genes, glcA and glcB, coding for the glucose-specific PTS transporters EIIGlc1 and EIIGlc2 which are 69% identical. The translation products derived from the nucleotide sequence consist of 675 and 692 amino acid residues and have calculated molecular weights of 73 025 and 75 256, respectively. Both genes can be stably maintained in Escherichia coli cells and restore the ability to ferment glucose to ptsG deletion mutants of E. coli. This demonstrates the ability of the PTS proteins HPr and/or EIIAGlc of a gram-negative organism (E. coli) to phosphorylate an EIICBAGlc from a gram-positive organism (S. carnosus).
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 250 (1996), S. 375-379 
    ISSN: 1617-4623
    Schlagwort(e): Glucose transporter ; Phosphotransferase system ; Membrane proteins ; glcA/B ; Staphylococcus carnosus
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Phosphoenolpyruvate (PEP)-dependent phosphorylation experiments have indicated that the grampositive bacteriumStaphylococcus carnosus possesses an EIICBA fusion protein specific for glucose. Here we report the cloning of a 7 kb genomic DNA fragment containing two genes,glcA andglcB, coding for the glucose-specific PTS transporters EIIGlc1 and EIIGlc2 which are 69% identical. The translation products derived from the nucleotide sequence consist of 675 and 692 amino acid residues and have calculated molecular weights of 73 025 and 75 256, respectively. Both genes can be stably maintained inEscherichia coli cells and restore the ability to ferment glucose toptsG deletion mutants ofE. coli. This demonstrates the ability of the PTS proteins HPr and/or EIIAGlc of a gram-negative organism (E. coli) to phosphorylate an EIICBAGlc from a gram-positive organism (S. carnosus).
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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