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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 111 (1976), S. 85-91 
    ISSN: 1432-072X
    Keywords: Ammonium metabolism ; Ammonium transport ; Glutamine synthetase ; Nitrogenase ; Glutamate synthase ; Glutamate dehydrogenase ; Nitrate reductase (dissimilatory) ; Klebsiella pneumoniae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The primary steps of N2, ammonia and nitrate metabolism in Klebsiella pneumoniae grown in a continuous culture are regulated by the kind and supply of the nitrogenous compound. Cultures growing on N2 as the only nitrogen source have high activities of nitrogenase, unadenylated glutamine synthetase and glutamate synthase and low levels of glutamate dehydrogenase. If small amounts of ammonium salts are added continuously, initially only part of it is absorbed by the organisms. After 2–3 h complete absorption of ammonia against an ammonium gradient coinciding with an increased growth rate of the bacteria is observed. The change in the extracellular ammonium level is paralleled by the intracellular glutamine concentration which in turn regulates the glutamine synthetase activity. An increase in the degree of adenylation correlates with a repression of nitrogenase synthesis and an induction of glutamate dehydrogenase synthesis. Upon deadenylation these events are reversed.—After addition of nitrate ammonia appears in the medium, probably due to the action of a membrane bound dissimilatory nitrate reductase.—Addition of dinitrophenol causes transient leakage of intracellular ammonium into the medium.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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