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We show that aminoglycosides can be doubly modified by the sequential actions of AMEs, with the activity of the second AME in most cases unaffected, decreased, or completely abolished. We demonstrate that the bifunctional enzyme AAC(3)-Ib\/AAC(6\u2032)-Ib\u2032 can diacetylate gentamicin. Since single acetylation does not always inactivate the parent drugs completely, two modifications likely provide more-robust inactivation\n            <jats:italic>in vivo<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/aac.00312-11","type":"journal-article","created":{"date-parts":[[2011,5,3]],"date-time":"2011-05-03T02:42:03Z","timestamp":1304390523000},"page":"3207-3213","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":35,"title":["Effects of Altering Aminoglycoside Structures on Bacterial Resistance Enzyme Activities"],"prefix":"10.1128","volume":"55","author":[{"given":"Keith D.","family":"Green","sequence":"first","affiliation":[{"name":"Life Sciences Institute, 210 Washtenaw Ave., Ann Arbor Michigan 48109-2216"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wenjing","family":"Chen","sequence":"additional","affiliation":[{"name":"Chemical Biology Doctoral Program, 210 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