Regulation of glutamate dehydrogenase in Bacillus subtilis.
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.
D050788:Alanine Dehydrogenase; D000594:Amino Acid Oxidoreductases / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology* / Q000502:physiology; D003470:Culture Media; D004790:Enzyme Induction; D004794:Enzyme Repression; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D005971:Glutamates / Q000378:metabolism*; D018698:Glutamic Acid; D013171:Spores, Bacterial / Q000502:physiology
D003470:Culture Media; D005971:Glutamates; D018698:Glutamic Acid; D000594:Amino Acid Oxidoreductases; D050788:Alanine Dehydrogenase; D005969:Glutamate Dehydrogenase