Author:
Kane J F,Wakim J,Fischer R S
Abstract
The activity of the nicotinamide adenine dinucleotide-dependent glutamate dehydrogenase in Bacillus subtilis was influenced by the carbon source, but not the nitrogen source, in the growth medium. The highest specific activity for this enzyme was found when B. subtilis was grown in a minimal or rich medium that contained glutamate as the carbon source. It is proposed that glutamate dehydrogenase serves a catabolic function in the metabolism of glutamate, is induced by glutamate, and is subject to catabolite repression.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference24 articles.
1. Aronson J. N. 1976. Ammonia assimilation and glutamate catabolism by Bacillus thuringiensis p. 444-449. In D. Schlessinger (ed.) Microbiology-1976. American Society for Microbiology Washington D.C.
2. Glutamate dehydrogenase genetic mapping and isolation of regulatory mutants of Klebsiella aerogenes;Bender R. A.;J. Bacteriol.,1976
3. Regulation of the ammonia asimilatory enzymes in Salmonella typhimurium;Brenchley J. E.;J. Bacteriol.,1975
4. Mutants of KlebsieUa aerogenes lacking glutamate dehydrogenase;Brenchley J. E.;J. Bacteriol.,1974
5. Role of glutamate in the sporogenesis ofBacillus cereus;Charba J. F.;J. Bacteriol.,1977
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