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  • 1
    Electronic Resource
    Electronic Resource
    Structure and function of proteins of the phosphotransferase system and of 6-phospho-β-glycosidases in Gram-positive bacteria (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 12 (1993), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract: New information about the proteins of the phosphotransferase system (PTS) and of phosphoglycosidases of homofermentative lactic acid bacteria and related species is presented. Tertiary structures were elucidated from soluble PTS components. They help to understand regulatory processes and PTS function in lactic acid bacteria. A tertiary structure of a membrane-bound enzyme II is still not available, but expression of Gram-positive genes encoding enzymes II can be achieved in Escherichia coli and enables the development of effective isolation procedures which are necessary for crystallization experiments. Considerable progress was made in analysing the functions of structural genes which are in close vicinity of the genes encoding the sugar-specific PTS components, such as the genes encoding the tagatose-6-P pathway and the 6-phospho-β-glycosidases. These phosphoglycosidases belong to a subfamily of the β-glycosidase family I among about 300 different glycosidases. The active site nucleophile was recently identified to be Glu 358 in Agrobacteriumβ-glucosidase. This corresponds to Glu 375 in staphylococcal and lactococcal 6-phospho-β-galactosidase. This enzyme is inactivated by mutating Glu 375 to Gln. Diffracting crystals of the lactococcal 6-P-β-galactosidase allow the elucidation of its tertiary structure which helps to derive the structures for the entire glycosidase family 1. In addition, a fusion protein with 6-phospho-β-galactosidase and staphylococcal protein A was constructed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.1993.tb00016.x
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning and sequencing of two genes from Staphylococcus carnosus coding for glucose-specific PTS and their expression in Escherichia coli K-12 (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 375-379 
    Details
    ISSN: 1617-4623
    Keywords: Key words Glucose transporter ; Phosphotransferase system ; Membrane proteins ; glcA/B ; Staphylococcus carnosus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02174396
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