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Among them, OXA-181 and OXA-232 are of particular interest, as they differ from each other by a single amino acid substitution at position 214 (R in OXA-181 and S in OXA-232) that results in reduced carbapenem-hydrolyzing activity for OXA-232. To investigate the role of amino acid position 214 (AA214), the X-ray structure of OXA-232 was determined and AA214 of OXA-48 and of OXA-232 was replaced by G, L, D, E, S, R, and K using site-directed mutagenesis.\n          <\/jats:p>","DOI":"10.1128\/aac.02329-19","type":"journal-article","created":{"date-parts":[[2020,2,13]],"date-time":"2020-02-13T14:14:15Z","timestamp":1581603255000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":40,"title":["Role of Arginine 214 in the Substrate Specificity of OXA-48"],"prefix":"10.1128","volume":"64","author":[{"given":"Saoussen","family":"Oueslati","sequence":"first","affiliation":[{"name":"EA7361 Structure, Dynamic, Function and Expression of Broad Spectrum \u03b2-Lactamases, UMR1184, Faculty of Medicine, LabEx LERMIT, Universit\u00e9 Paris-Saclay, Le Kremlin-Bic\u00eatre, 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