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
