[Metabolism of dicarboxylic amino acids and their amides in bacteria of the genus Citrobacter].

In 58 Citrobacter strains the pathways of the utilization of dicarbonic amino acids and their amides were studied. These organisms were found to be incapable of decarboxylating glutaminic and asparaginic acids, as well as their amides. All the strains could actively desamidizate asparagine. Not all of these strains showed glutaminase activity. Aspartate-aminotransferase occurred twice as often as alanine-aminotransferase, the level of activity being approximately the same. The Citrobacter strains desamidizated asparaginic acid with great constancy, but only in 1/3 of them this reaction occurred via an aspartase route. The desamidization of asparaginic acid in Citrobacter seemed to proceed in different ways. The desamidization of glutaminic acid was observed only in a part of the strains, and the reaction proceeded less actively.