Sodium effect of growth on aspartate and genetic analysis of a Bacillus subtilis mutant with high aspartase activity.
Most strains of Bacillus subtilis, dervied from the 168 (Marburg) strain, grow slowly on aspartate as sole carbon source. We isolated a mutant (aspH) that grows rapidly on aspartate because it produces aspartase constitutively. Thus, aspartase is needed for rapid growth on aspartate, whereas aspartate-alpha-ketoglutarate aminotransferase is not needed, as was demonstrated by a mutant lacking that enzyme activity. By two--and three-factor crosses using PBSl transduction, the aspH mutation was located between the aroD and the lys markers of the genetic map. Although sodium ions do not affect growth on glucose or L-malate, they specifically stimulate growth on aspartate in both the parent and the aspH mutant strains. Enzyme activities of crude aspartase and fumarase and of purified aspartase do not increase in the presence of sodium. These results show that stimulation by sodium involves some reaction other than the enzymes catabolizing aspartate. The ease of purification from the aspH strain and the stability of aspartase suggest that the B. subtilis enzyme is particularly useful for aspartate determinations.
D000642:Ammonia-Lyases / Q000096:biosynthesis*; D001220:Aspartate Ammonia-Lyase / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D001224:Aspartic Acid / Q000378:metabolism*; D001412:Bacillus subtilis / Q000187:drug effects / Q000378:metabolism*; D002874:Chromosome Mapping; D002876:Chromosomes, Bacterial; D005796:Genes; D011188:Potassium / Q000494:pharmacology; D012964:Sodium / Q000494:pharmacology*
D001224:Aspartic Acid; D012964:Sodium; D000642:Ammonia-Lyases; D001220:Aspartate Ammonia-Lyase; D011188:Potassium