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Regulation of ammonium assimilation by Clostridium acetobutylicum
Author(s) -
Amine J.,
Marczak R.,
Maazouzi N.,
Masion E.
Publication year - 1990
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620300904
Subject(s) - clostridium acetobutylicum , glutamine synthetase , glutamate synthase , biochemistry , ammonium , glutamate dehydrogenase , ammonium chloride , glutamine , asparagine synthetase , chemistry , asparagine , glutamine amidotransferase , enzyme , ammonia , biosynthesis , assimilation (phonology) , glutamate receptor , amino acid , butanol , organic chemistry , ethanol , receptor , linguistics , philosophy
Assimilation of ammonium by the obligate anaerobic bacterium Clostridium acetobutylicum was accomplished by the pathway: Glutamine synthetase/glutamate synthase. C. acetobutylicum also contained an asparagine synthetase, but no glutamate dehydrogenase activity was detected. The glutamine synthetase was partially repressed by addition of large amounts of ammonium chloride and/or casaminoacids to the medium, while the biosynthesis of the other enzymes was not regulated by the extracellular concentration of ammonium.