{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T12:48:42Z","timestamp":1762865322671},"reference-count":12,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2007,12,1]],"date-time":"2007-12-01T00:00:00Z","timestamp":1196467200000},"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":[[2007,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The carbapenem-hydrolyzing \u03b2-lactamase SFC-1 from\n            <jats:italic>Serratia fonticola<\/jats:italic>\n            UTAD54 was overexpressed in\n            <jats:italic>Escherichia coli<\/jats:italic>\n            , purified, and characterized. The enzyme exhibited an apparent molecular mass of 30.5 kDa, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. SFC-1 hydrolyzes penicillins, cephalosporins, aztreonam, and carbapenems and is inhibited by clavulanic acid, sulbactam, and tazobactam.\n          <\/jats:p>","DOI":"10.1128\/aac.00491-07","type":"journal-article","created":{"date-parts":[[2007,9,18]],"date-time":"2007-09-18T01:20:04Z","timestamp":1190078404000},"page":"4512-4514","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":22,"title":["Biochemical Characterization of SFC-1, a Class A Carbapenem-Hydrolyzing \u03b2-Lactamase"],"prefix":"10.1128","volume":"51","author":[{"given":"Fa\u0301tima","family":"Fonseca","sequence":"first","affiliation":[{"name":"Centre for Environmental and Marine Studies and Department of Biology, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Ana Cristina","family":"Sarmento","sequence":"additional","affiliation":[{"name":"Centre for Environmental and Marine Studies and Department of Biology, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Isabel","family":"Henriques","sequence":"additional","affiliation":[{"name":"Centre for Environmental and Marine Studies and Department of Biology, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Bart","family":"Samyn","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Physiology and Microbiology, Laboratory of Protein Biochemistry and Protein Engineering, Ghent University, Ghent, Belgium"}]},{"given":"Jozef","family":"van Beeumen","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Physiology and Microbiology, Laboratory of Protein Biochemistry and Protein Engineering, Ghent University, Ghent, Belgium"}]},{"given":"Pedro","family":"Domingues","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Maria Rosa\u0301rio","family":"Domingues","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Maria Jose\u0301","family":"Saavedra","sequence":"additional","affiliation":[{"name":"Department of Veterinary Science, Center of Studies in Animal and Veterinary Science, University of Tra\u0301s-os-Montes e Alto Douro, 5001-801 Vila Real, Portugal"}]},{"given":"Anto\u0301nio","family":"Correia","sequence":"additional","affiliation":[{"name":"Centre for Environmental and Marine Studies and Department of Biology, University of Aveiro, 3810-193 Aveiro, Portugal"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.48.6.2321-2324.2004"},{"key":"e_1_3_2_3_2","first-page":"29","volume":"143","year":"1996","unstructured":"Mariotte-Boyer, S., M. H. Nicolas-Chanoine, and R. Labia. 1996. A kinetic study of NMC-A \u03b2-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins. FEMS Microbiol. Lett.143:29-33.","journal-title":"FEMS Microbiol. 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