{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T13:33:24Z","timestamp":1762868004110},"reference-count":51,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[1998,2,1]],"date-time":"1998-02-01T00:00:00Z","timestamp":886291200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[1998,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:italic>Klebsiella aerogenes<\/jats:italic>\n            strains with reduced levels of\n            <jats:sc>d<\/jats:sc>\n            -amino acid dehydrogenase not only fail to use alanine as a growth substrate but also become sensitive to alanine in minimal media supplemented with glucose and ammonium. The inability of these mutant strains to catabolize the alanine provided in the medium interferes with both pathways of glutamate production. Alanine derepresses the nitrogen regulatory system (Ntr), which in turn represses glutamate dehydrogenase, one pathway of glutamate production. Alanine also inhibits the enzyme glutamine synthetase, the first enzyme in the other pathway of glutamate production. Therefore, in the presence of alanine, strains with mutations in\n            <jats:italic>dadA<\/jats:italic>\n            (the gene that codes for a subunit of the dehydrogenase) exhibit a glutamate auxotrophy when ammonium is the sole source of nitrogen. The alanine catabolic operon of\n            <jats:italic>Klebsiella aerogenes<\/jats:italic>\n            ,\n            <jats:italic>dadAB<\/jats:italic>\n            , was cloned, and its DNA sequence was determined. The clone complemented the alanine defects of\n            <jats:italic>dadA<\/jats:italic>\n            strains. The operon has a high similarity to the\n            <jats:italic>dadAB<\/jats:italic>\n            operon of\n            <jats:italic>Salmonella typhimurium<\/jats:italic>\n            and the\n            <jats:italic>dadAX<\/jats:italic>\n            operon of\n            <jats:italic>Escherichia coli<\/jats:italic>\n            , each of which codes for the smaller subunit of\n            <jats:sc>d<\/jats:sc>\n            -amino acid dehydrogenase and the catabolic alanine racemase. Unlike the cases for\n            <jats:italic>E. coli<\/jats:italic>\n            and\n            <jats:italic>S. typhimurium<\/jats:italic>\n            , the\n            <jats:italic>dad<\/jats:italic>\n            operon of\n            <jats:italic>K. aerogenes<\/jats:italic>\n            is activated by the Ntr system, mediated in this case by the nitrogen assimilation control protein (NAC). A sequence matching the DNA consensus for NAC-binding sites is located centered at position \u221244 with respect to the start of transcription. The promoter of this operon also contains consensus binding sites for the catabolite activator protein and the leucine-responsive regulatory protein.\n          <\/jats:p>","DOI":"10.1128\/jb.180.3.563-570.1998","type":"journal-article","created":{"date-parts":[[2019,12,31]],"date-time":"2019-12-31T16:30:04Z","timestamp":1577809804000},"page":"563-570","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":44,"title":["Alanine Catabolism in\n            <i>Klebsiella aerogenes<\/i>\n            : Molecular Characterization of the\n            <i>dadAB<\/i>\n            Operon and Its Regulation by the Nitrogen Assimilation Control Protein"],"prefix":"10.1128","volume":"180","author":[{"given":"Brian K.","family":"Janes","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Department of Biology, The University of Michigan, Ann Arbor, Michigan 48109-1048"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert A.","family":"Bender","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Biology, The University of Michigan, Ann Arbor, Michigan 48109-1048"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","unstructured":"Ausubel\nF. 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