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. 1970 May;102(2):524–530. doi: 10.1128/jb.102.2.524-530.1970

Mutants of Salmonella typhimurium Lacking Phosphoenolpyruvate Carboxykinase and α-Ketoglutarate Dehydrogenase Activities

Guillermo Carrillo-Castañeda 1, Manuel V Ortega 1
PMCID: PMC247580  PMID: 4911543

Abstract

Two auxotrophic mutants (SM16 and SM51) of Salmonella typhimurium, which for aerobic growth, with hexoses as carbon source, required lysine and methionine (SM51 required also nicotinic acid), were isolated and characterized. The requirement for the amino acids disappeared in anaerobiosis. Neither lipoate nor 4-hydroxybenzoate was effective in supporting aerobic growth of the mutants. The lysine and methionine requirement for aerobic growth was due to the absence in the mutants of the enzymatic activities of the α-ketoglutarate dehydrogenase complex. The mutants could not use succinate as carbon source even after enrichment of the growth medium with acid-hydrolyzed casein and yeast extract. No phosphoenolpyruvate carboxykinase activity was found in the mutants, a phenomenon which explained their inability to use succinate. By interrupted conjugation and by transduction experiments, the positions of the three affected loci, pck, suc, and Nic, were located at approximately 17 to 19 min of the S. typhimurium chromosome; they were found to be closely linked. From different criteria, it appears as if the genetic lesions present in both mutants are due to deletion of a small chromosome fragment.

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Selected References

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