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  • 1
    Electronic Resource
    Electronic Resource
    Pathways and regulation of N2, ammonium and glutamate assimilation by Clostridium formicoaceticum (1983)
    Springer
    Archives of microbiology 134 (1983), S. 167-169 
    Details
    ISSN: 1432-072X
    Keywords: Nitrogenase ; Glutamine synthetase ; Glutamate synthase ; Glutamate dehydrogenase ; Asparagine synthetase ; Alanine dehydrogenase ; β-Methylaspartase ; Clostridium formicoaceticum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Clostridium formicoaceticum possesses the following enzymes for the assimilation of N2 and NH 4 + : nitrogenase, glutamine synthetase, NADH- and NADPH-dependent glutamate synthase, NADH- and NADPH-dependent glutamate dehydrogenase, NADPH-dependent alamine dehydrogenase, and NH 4 + -dependent asparagine synthetase. Nitrogenase and glutamine synthetase are repressed and alanine dehydrogenase is induced by NH 4 + , while the synthesis of the other enzymes is not influenced by the extracellular NH 4 + level. Glutamate is degraded via glutamate mutase and β-methylaspartase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00407953
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  • 2
    Electronic Resource
    Electronic Resource
    Regulation of ammonium uptake and metabolism by nitrogen fixing bacteria. III. Clostridium pasteurianum (1979)
    Springer
    Archives of microbiology 120 (1979), S. 263-270 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00423074
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of a Paracoccus denitrificans mutant pleiotropically impaired in nitrogen metabolism (1993)
    Springer
    Archives of microbiology 160 (1993), S. 166-168 
    Details
    ISSN: 1432-072X
    Keywords: Paracoccus denitrificans ; Ammonia assimilation pathways ; Nitrogen catabolism regulation ; Ammonium transport ; Glutamine synthetase ; Glutamate synthase ; Aminotransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A Tn5 insertional prototrophic mutant of Paracoccus denitrificans (UBM219) was generated which grew on high (〉1 mM) but not low (〈0.5 mM) ammonium as sole nitrogen source. It did not utilize nitrate and most amino acids except glutamate and aspartate. UBM219 showed more than 10-fold lower levels of ammonium (methylammonium) transport, aspartate and alanine aminotransferase, but more than 10-fold higher activities of glutamate dehydrogenase and glutamate synthase. This pleiotropy indicates a mutation in a regulatory gene affecting nitrogen metabolism in general. — Ammonia assimilation pathways and regulation in Paracoccus resemble the patterns in enterobacteria with the exception, that alanine is generated by amino transfer from glutamate to pyruvate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00288721
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  • 4
    Electronic Resource
    Electronic Resource
    Ammonium uptake and metabolism by nitrogen fixing bacteria (1976)
    Springer
    Archives of microbiology 111 (1976), S. 85-91 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00446553
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  • 5
    Electronic Resource
    Electronic Resource
    Relationships between nitrogenase, glutamine synthetase, glutamine, and energy charge in Azotobacter vinelandii (1981)
    Springer
    Archives of microbiology 128 (1981), S. 412-415 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00405923
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    Paper (German National Licenses)
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