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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 120 (1979), S. 263-270 
    ISSN: 1432-072X
    Keywords: Enzyme regulation ; Ammonium metabolism ; Nitrogenase ; Glutamine synthetase ; Glutamate synthase ; Glutamate dehydrogenase ; Asparagine synthetase ; Amino acid pools ; Clostridium pasteurianum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Addition of ammonium salts to N2 fixing continuous cultures of Clostridium pasteurianum caused immediate stop of nitrogenase synthesis, while the levels of glutamine synthetase, glutamate dehydrogenase and asparagine synthetase remained constant. No evidence for an interconversion of the glutamine synthetase was found. The activities of glutamate synthase in crude extracts were inversely related to the nitrogenase levels. The intracellular glutamine pool rapidly expanded during nitrogenase repression and decreased as fast during derepression while the pool sizes of all other amino acids were not strongly related to the rate of nitrogenase formation. These investigations suggest glutamine as corepressor of nitrogenase synthesis.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 128 (1981), S. 412-415 
    ISSN: 1432-072X
    Keywords: Nitrogenase ; Glutamine synthetase ; Repression ; Amino acid pools ; Adenine nucleotide pools ; Azolobacter vinelandii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When continuous cultures of Azotobacter vinelandii were supplied with ammonium or nitrate in amounts, which just repressed nitrogenase synthesis completely, both the intracellular glutamine level and the degree of adenylylation of the glutamine synthetase (GS) increased only slightly (from 0.45–0.50 mM and from 2 to 3 respectively), while the total GS level remained unaffected. Higher amounts of ammonium additionally inhibited the nitrogenase activity, caused a strong rise in the intracellular glutamine concentration and adenylylation of the GS, but caused no change in the ATP/ADP ratio. These results are considered as evidence that in A. vinelandii the regulation of nitrogenase synthesis is not linked to the adenylylation state of the GS and to the intracellular glutamine level, and that the inhibition of the nitrogenase activity as a consequence of a high extracellular ammonium level is not mediated via a change in the energy charge.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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