{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T22:23:17Z","timestamp":1785882197076,"version":"3.56.0"},"reference-count":60,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2014,10,12]],"date-time":"2014-10-12T00:00:00Z","timestamp":1413072000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2014,11]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Aminotransferases can be redundant or promiscuous, but the extent and significance of these properties is not known in any organism, even in <jats:styled-content style=\"fixed-case\"><jats:italic>E<\/jats:italic><\/jats:styled-content><jats:italic>scherichia coli<\/jats:italic>. To determine the extent of redundancy, it was first necessary to identify the redundant aminotransferases in arginine and lysine synthesis, and then complement all aminotransferase\u2010deficient mutants with genes for all aminotransferases. The enzymes with <jats:italic>N<\/jats:italic>\u2010acetylornithine aminotransferase (<jats:styled-content style=\"fixed-case\">ACOAT<\/jats:styled-content>) activity in arginine synthesis were <jats:styled-content style=\"fixed-case\">ArgD<\/jats:styled-content>, <jats:styled-content style=\"fixed-case\">AstC<\/jats:styled-content>, <jats:styled-content style=\"fixed-case\">GabT<\/jats:styled-content> and <jats:styled-content style=\"fixed-case\">PuuE<\/jats:styled-content>; the major anaerobic <jats:styled-content style=\"fixed-case\">ACOAT<\/jats:styled-content> was <jats:styled-content style=\"fixed-case\">ArgD<\/jats:styled-content>. The major enzymes with <jats:styled-content style=\"fixed-case\"><jats:italic>N<\/jats:italic><\/jats:styled-content>\u2010succinyl\u2010<jats:sc>l<\/jats:sc>,<jats:sc>l<\/jats:sc>\u2010diaminopimelate aminotransferase (<jats:styled-content style=\"fixed-case\">SDAP<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">AT<\/jats:styled-content>) activity in lysine synthesis were <jats:styled-content style=\"fixed-case\">ArgD<\/jats:styled-content>, <jats:styled-content style=\"fixed-case\">AstC<\/jats:styled-content>, and <jats:styled-content style=\"fixed-case\">SerC<\/jats:styled-content>. Seven other aminotransferases, when overproduced, complemented the defect in a triple mutant. Lysine availability did not regulate synthesis of the major <jats:styled-content style=\"fixed-case\">SDAP<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">ATs<\/jats:styled-content>. Complementation analysis of mutants lacking aminotransferases showed that the <jats:styled-content style=\"fixed-case\">SDAP<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">ATs<\/jats:styled-content> and alanine aminotransferases were exceptionally redundant, and it is proposed that this redundancy may ensure peptidoglycan synthesis. An overview of all aminotransferase reactions indicates that redundancy and broad specificity are common properties of aminotransferases.<\/jats:p>","DOI":"10.1111\/mmi.12801","type":"journal-article","created":{"date-parts":[[2014,9,22]],"date-time":"2014-09-22T06:12:07Z","timestamp":1411366327000},"page":"843-856","source":"Crossref","is-referenced-by-count":37,"title":["The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in <scp><i>E<\/i><\/scp><i>scherichia coli<\/i>"],"prefix":"10.1111","volume":"94","author":[{"given":"Piyush Behari","family":"Lal","sequence":"first","affiliation":[{"name":"Department of Molecular and Cell Biology The University of Texas at Dallas  Richardson TX 75080 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbara L.","family":"Schneider","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology The University of Texas at Dallas  Richardson TX 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