{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,7,15]],"date-time":"2024-07-15T03:01:11Z","timestamp":1721012471338},"reference-count":32,"publisher":"American Society for Microbiology","issue":"8","license":[{"start":{"date-parts":[[2013,8,1]],"date-time":"2013-08-01T00:00:00Z","timestamp":1375315200000},"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":[[2013,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            SGM-1 is a novel class A \u03b2-lactamase from an environmental isolate of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Sphingobium<\/jats:named-content>\n            sp. containing all of the distinct amino acid motifs of class A \u03b2-lactamases. It shares 77 to 80% amino acid sequence identity with putative \u03b2-lactamases that are present on the chromosome of all\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Sphingobium<\/jats:named-content>\n            species whose genomes were sequenced and annotated. Thus, SGM-type \u03b2-lactamases are native to this genus. Antibiotic susceptibility testing classifies SGM-1 as an extended-spectrum \u03b2-lactamase, conferring the highest level of resistance to penicillins. Although SGM-1 contains the conserved cysteine residues characteristic of class A carbapenemases, it does not confer resistance to the carbapenem antibiotics imipenem, meropenem, or doripenem but does increase the MIC of ertapenem 8-fold. SGM-1 hydrolyzes penicillins and the monobactam aztreonam with similar catalytic efficiencies, ranging from 10\n            <jats:sup>5<\/jats:sup>\n            to 10\n            <jats:sup>6<\/jats:sup>\n            M\n            <jats:sup>\u22121<\/jats:sup>\n            s\n            <jats:sup>\u22121<\/jats:sup>\n            . The catalytic efficiencies of SGM-1 for cefoxitin and ceftazidime were the lowest (10\n            <jats:sup>2<\/jats:sup>\n            to 10\n            <jats:sup>3<\/jats:sup>\n            M\n            <jats:sup>\u22121<\/jats:sup>\n            s\n            <jats:sup>\u22121<\/jats:sup>\n            ) among the cephalosporins tested, while the catalytic efficiencies against all other cephalosporins varied from about 10\n            <jats:sup>5<\/jats:sup>\n            to 10\n            <jats:sup>6<\/jats:sup>\n            M\n            <jats:sup>\u22121<\/jats:sup>\n            s\n            <jats:sup>\u22121<\/jats:sup>\n            . SGM-1 exhibited measurable but not significant activity toward the carbapenems tested. SGM-1 also showed high affinity for clavulanic acid, tazobactam, and sulbactam (\n            <jats:italic>\n              K\n              <jats:sub>i<\/jats:sub>\n            <\/jats:italic>\n            &lt; 1 \u03bcM); however, only clavulanic acid significantly reduced the MICs of \u03b2-lactams.\n          <\/jats:p>","DOI":"10.1128\/aac.00808-13","type":"journal-article","created":{"date-parts":[[2013,5,29]],"date-time":"2013-05-29T04:58:59Z","timestamp":1369803539000},"page":"3783-3788","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":10,"title":["A Novel Extended-Spectrum \u03b2-Lactamase, SGM-1, from an Environmental Isolate of Sphingobium sp"],"prefix":"10.1128","volume":"57","author":[{"given":"Toni L.","family":"Lamoureaux","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Viktoria","family":"Vakulenko","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marta","family":"Toth","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hilary","family":"Frase","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sergei B.","family":"Vakulenko","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/nyas.12023"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.coph.2007.08.003"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00037-09"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.00961-09"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.00223-12"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/dkm226"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.49.9.3743-3748.2005"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.44.3.622-632.2000"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.05305-11"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M109.011262"},{"key":"e_1_3_2_12_2","volume-title":"Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically; approved standard","author":"Clinical and Laboratory Standards Institute","year":"2009","unstructured":"Clinical and Laboratory Standards Institute. 2009. 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