{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,10]],"date-time":"2026-04-10T20:26:47Z","timestamp":1775852807789,"version":"3.50.1"},"reference-count":39,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"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":[[2006,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:italic>Morganella morganii<\/jats:italic>\n            produces an inducible, chromosomally encoded AmpC \u03b2-lactamase. We describe in this study three new variants of AmpC within this species with apparent pIs of 6.6 (M19 from\n            <jats:italic>M. morganii<\/jats:italic>\n            strain PP19), 7.4 (M29 from\n            <jats:italic>M. morganii<\/jats:italic>\n            strain PP29), and 7.8 (M37 from\n            <jats:italic>M. morganii<\/jats:italic>\n            strain PP37). After gene sequencing, deduced amino acid sequences displayed one to six substitutions when compared to the available\n            <jats:italic>Morganella<\/jats:italic>\n            AmpC sequences. An AmpR-encoding gene was also found upstream of\n            <jats:italic>ampC<\/jats:italic>\n            , including the LysR regulators' helix-turn-helix DNA-binding domain and the putative T-N\n            <jats:sub>11<\/jats:sub>\n            -A-protected region in the\n            <jats:italic>ampR-ampC<\/jats:italic>\n            intercistronic sequence. All three AmpC variants were purified from in vitro-generated derepressed mutants and showed overall similar kinetic parameters. None of the observed amino acid changes, occurring at the surface of the protein, appear to have a major influence in their catalytic properties.\n            <jats:italic>Morganella<\/jats:italic>\n            AmpCs exhibit the highest catalytic efficiencies (\n            <jats:italic>\n              k\n              <jats:sub>cat<\/jats:sub>\n            <\/jats:italic>\n            \/\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            ) on classical penicillins, cefoxitin, narrow-spectrum cephalosporins, and cefotaxime. Cefotaxime was more effectively hydrolyzed than other oxyimino-cephalosporins, whereas cefepime was 3 log-fold less efficiently hydrolyzed than other cephalosporins such as cephalothin. Several differences with other AmpC \u03b2-lactamases were found. Ampicillin was more efficiently hydrolyzed than benzylpenicillin. High\n            <jats:italic>\n              k\n              <jats:sub>cat<\/jats:sub>\n            <\/jats:italic>\n            <jats:italic>\n              \/K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            values were observed for oxacillin and piperacillin, which are usually poor substrates for AmpC. A fairly efficient hydrolysis of imipenem was detected as well. Aztreonam, carbenicillin, and tazobactam were effective transient inactivators of these variants.\n          <\/jats:p>","DOI":"10.1128\/aac.50.3.962-967.2006","type":"journal-article","created":{"date-parts":[[2006,2,22]],"date-time":"2006-02-22T07:32:35Z","timestamp":1140593555000},"page":"962-967","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":31,"title":["Biochemical and Molecular Characterization of Three New Variants of AmpC \u03b2-Lactamases from\n            <i>Morganella morganii<\/i>"],"prefix":"10.1128","volume":"50","author":[{"given":"Pablo","family":"Power","sequence":"first","affiliation":[{"name":"Ca\u0301tedra de Microbiologi\u0301a, Facultad de Farmacia y Bioqui\u0301mica, Universidad de Buenos Aires, Juni\u0301n 954, Buenos Aires 1113, Argentina;"},{"name":"Centre d'Inge\u0301nierie des Prote\u0301ines, Universite\u0301 de Lie\u0300ge, Institut de Chimie, B6 (B4000), Sart Tilman, Belgium;"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Moreno","family":"Galleni","sequence":"additional","affiliation":[{"name":"Centre d'Inge\u0301nierie des Prote\u0301ines, Universite\u0301 de Lie\u0300ge, Institut de Chimie, B6 (B4000), Sart Tilman, Belgium;"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Juan A.","family":"Ayala","sequence":"additional","affiliation":[{"name":"Centro de Biologi\u0301a Molecular \u201cSevero Ochoa,\u201d CSIC-UAM, Campus de Cantoblanco 28049, Madrid, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gabriel","family":"Gutkind","sequence":"additional","affiliation":[{"name":"Ca\u0301tedra de Microbiologi\u0301a, Facultad de Farmacia y Bioqui\u0301mica, Universidad de Buenos Aires, Juni\u0301n 954, Buenos Aires 1113, Argentina;"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/25.2.199"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.48.2.533-537.2004"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-1097(97)00006-2"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.42.9.2352"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1993.tb00927.x"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.180.3.647-654.1998"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.6.1211"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-2952(87)90609-5"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/22.Supplement_A.37"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1099\/13500872-141-2-419"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/47.2.207"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/39.1.85"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2550123"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2550119"},{"key":"e_1_3_2_16_2","unstructured":"Gerhardt P. 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