2-Ketoglutarate and the regulation of aconitase and histidase formation in Bacillus subtilis.
In contrast to wild-type cells, the Bacillus subtilis mutant SF109 that lacks the active 2-ketoglutarate dehydrogenase enzymatic complex is unable to increase the specific activity of two enzymes subject to glucose catabolite repression, aconitase and histidase, during limitation of growth by glucose. Examination of the intracellular metabolite pools in the mutant and wild-type cells grown in excess and limiting glucose medium showed that the complete derepression of aconitase and histidase could be correlated with the decrease in the intracellular concentration of 2-ketoglutarate. The complete repression of aconitase that occurred in wild-type and mutant cells could be correlated with a high intracellular concentration of 2-ketoglutarate.
D000154:Aconitate Hydratase / Q000096:biosynthesis*; D000642:Ammonia-Lyases / Q000096:biosynthesis*; D001224:Aspartic Acid / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D004794:Enzyme Repression; D005947:Glucose / Q000378:metabolism; D005971:Glutamates / Q000378:metabolism; D018698:Glutamic Acid; D006638:Histidine Ammonia-Lyase / Q000096:biosynthesis*; D007656:Ketoglutaric Acids / Q000378:metabolism*; D009154:Mutation
D005971:Glutamates; D007656:Ketoglutaric Acids; D001224:Aspartic Acid; D018698:Glutamic Acid; D000154:Aconitate Hydratase; D000642:Ammonia-Lyases; D006638:Histidine Ammonia-Lyase; D005947:Glucose