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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 136 (1983), S. 297-299 
    ISSN: 1432-072X
    Keywords: Antibiotics ; β-Lactams ; Murein synthesis ; Ether treated bacteria ; Escherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The in vitro synthesis of murein from the precursors UDP-N-acetylglucosamine, l-alanine, d-glutamic acid and meso-diaminopimelic acid was performed with the aid of ether treated Escherichia coli. This synthesis was sensitive to representative inhibitors of early reactions in the cytoplasm as well as of late reactions in the membrane or the cell wall. The sensitivity was higher than in in vitro systems starting with UDP-N-acetylmuramic acid or UDP-N-acetylmuramylpentapeptide.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 144 (1986), S. 181-186 
    ISSN: 1432-072X
    Keywords: Antibiotics ; d-Amino acids ; ld-Carboxypeptidase ; Escherichia coli ; Murein synthesis ; Nocardicin A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A ld-carboxypeptidase from Escherichia coli K 12 was isolated by Tris-EDTA treatment and purified to electrophoretic homogeneity by DEAE-cellulose chromatography. The enzyme has a molecular weight of approximately 12,000 as determined by sodium dodecyl sulfatepolyacrylamide electrophoresis and by Sephadex G-100 gel filtration. The studies of the substrate specificity of the enzyme revealed that UDP-MurNAc-tetrapeptide is a superior substrate, with a K m value of 1×10-4 mol/l. The activity of the ld-carboxypeptidase was inhibited by d-amino acids and the β-lactam antibiotic nocardicin A. K i values of 0.3 and 43 mmol/l were determined for nocardicin A and d-homoserine, respectively. The properties of the purified enzyme correspond to activity I in ether treated cells.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 123 (1979), S. 275-279 
    ISSN: 1432-072X
    Keywords: Methanobacterium ; Methanosarcina barkeri ; Methanospirillum hungatii ; Cell wall ; Pseudomurein ; Sensitivity ; Antibiotics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The sensitivity to inhibitors of various steps of murein synthesis was studied with six strains of methanogenic bacteria. Four of the strains belong to the genus Methanobacterium, which contains pseudomurein in its cell walls. This polymer-as well as murein-is not present in the two control organisms, Methanosarcina barkeri and Methanospirillum hungatii, which were found to be resistant to all inhibitors of murein synthesis. The four strains of Methanobacterium were resistant to the antibiotics fosfomycin, D-cycloserine, vancomycin, penicillin G and cephalosporin C, all of which inhibit the synthesis or function of the peptide subunits of murein. On the other hand, the four strains were susceptible to bacitracin, nisin, gardimycin and enduracidin. It is therefore assumed that the biosynthesis of murein and pseudomurein, respectively, may have some reactions of the so-called lipid cycle and the polymerization of the heteroglycan strands in common.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 127 (1980), S. 187-193 
    ISSN: 1432-072X
    Keywords: Antibiotics ; Murein (peptidoglycan) synthesis ; Nisin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nisin inhibits murein synthesis with concomitant accumulation of undecaprenyl-pyrophospho-MurNAc(pentapeptide) (lipid intermediate I). This inhibition is caused by the formation of a complex between the antibiotic and lipid intermediate I. Undecaprenyl-pyrophospho-MurNAc(pentapeptide)-GlcNAc (lipid intermediate II) also forms a complex with nisin. However, when murein synthesis is inhibited by nisin, this latter complex is not formed since lipid intermediate II is no longer synthesized.
    Type of Medium: Electronic Resource
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