{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T12:10:53Z","timestamp":1791288653792,"version":"4.3.0"},"reference-count":28,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2012,6,1]],"date-time":"2012-06-01T00:00:00Z","timestamp":1338508800000},"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":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2012,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            FPH-1 is a new class A carbapenemase from\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Francisella philomiragia<\/jats:named-content>\n            . It produces high-level resistance to penicillins and the narrow-spectrum cephalosporin cephalothin and hydrolyzes these \u03b2-lactam antibiotics with catalytic efficiencies of 10\n            <jats:sup>6<\/jats:sup>\n            to 10\n            <jats:sup>7<\/jats:sup>\n            M\n            <jats:sup>\u22121<\/jats:sup>\n            s\n            <jats:sup>\u22121<\/jats:sup>\n            . When expressed in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n            , the enzyme confers resistance to clavulanic acid, tazobactam, and sulbactam and has\n            <jats:italic>\n              K\n              <jats:sub>i<\/jats:sub>\n            <\/jats:italic>\n            values of 7.5, 4, and 220 \u03bcM, respectively, against these inhibitors. FPH-1 increases the MIC of the monobactam aztreonam 256-fold and the MIC of the broad-spectrum cephalosporin ceftazidime 128-fold, while the MIC of cefoxitin remains unchanged. MICs of the carbapenem antibiotics imipenem, meropenem, doripenem, and ertapenem are elevated 8-, 8-, 16-, and 64-fold, respectively, against an\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            JM83 strain producing the FPH-1 carbapenemase. The catalytic efficiencies of the enzyme against carbapenems are in the range of 10\n            <jats:sup>4<\/jats:sup>\n            to 10\n            <jats:sup>5<\/jats:sup>\n            M\n            <jats:sup>\u22121<\/jats:sup>\n            s\n            <jats:sup>\u22121<\/jats:sup>\n            . FPH-1 is 77% identical to the FTU-1 \u03b2-lactamase from\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Francisella tularensis<\/jats:named-content>\n            and has low amino acid sequence identity with other class A \u03b2-lactamases. Together with FTU-1, FPH-1 constitutes a new branch of the prolific and ever-expanding class A \u03b2-lactamase tree.\n          <\/jats:p>","DOI":"10.1128\/aac.00223-12","type":"journal-article","created":{"date-parts":[[2012,3,27]],"date-time":"2012-03-27T02:53:37Z","timestamp":1332816817000},"page":"2852-2857","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":16,"title":["Class A Carbapenemase FPH-1 from Francisella philomiragia"],"prefix":"10.1128","volume":"56","author":[{"given":"Marta","family":"Toth","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Viktoria","family":"Vakulenko","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nuno T.","family":"Antunes","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hilary","family":"Frase","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergei B.","family":"Vakulenko","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2760269"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi200403e"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.05305-11"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.diagmicrobio.2007.02.013"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.mib.2010.09.006"},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/cc8892","article-title":"Bench-to-bedside review: the role of \u03b2-lactamases in antibiotic-resistant Gram-negative infections","volume":"14","author":"Bush K","year":"2010","unstructured":"BushK. 2010. 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