{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T06:56:14Z","timestamp":1790060174966,"version":"4.0.1"},"reference-count":38,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2002,6,1]],"date-time":"2002-06-01T00:00:00Z","timestamp":1022889600000},"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":[[2002,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>The sequenced chromosome of<jats:italic>Caulobacter crescentus<\/jats:italic>CB15 encodes a hypothetical protein that exhibits significant similarity (30 to 35% identical residues) to metallo-\u03b2-lactamases of subclass B3. An allelic variant of this gene (divergent by 3% of its nucleotides) was cloned in<jats:italic>Escherichia coli<\/jats:italic>from<jats:italic>C. crescentus<\/jats:italic>type strain DSM4727. Expression studies confirmed the metallo-\u03b2-lactamase activity of its product, CAU-1. The enzyme produced in<jats:italic>E. coli<\/jats:italic>was purified by two ion-exchange chromatography steps. CAU-1 contains a 29-kDa polypeptide with an alkaline isoelectric pH (&gt;9), and unlike the L1 enzyme of<jats:italic>Stenotrophomonas maltophilia<\/jats:italic>, the native form is monomeric. Kinetic analysis revealed a preferential activity toward penicillins, carbapenems, and narrow-spectrum cephalosporins, while oxyimino cephalosporins were poorly or not hydrolyzed. Affinities for the various \u03b2-lactams were poor overall (<jats:italic>K<jats:sub>m<\/jats:sub><\/jats:italic>values were always &gt;100 \u03bcM and often &gt;400 \u03bcM). The interaction with divalent ion chelators appeared to occur by a mechanism similar to that prevailing in other members of subclass B3. In<jats:italic>C. crescentus<\/jats:italic>, the CAU-1 enzyme is produced independently of \u03b2-lactam exposure and, interestingly, the<jats:italic>bla<\/jats:italic><jats:sub>CAU<\/jats:sub>determinant is bracketed by three other genes, including two genes encoding enzymes involved in methionine biosynthesis and a gene encoding a putative transcriptional regulator, in an operon-like structure. The CAU-1 enzyme is the first example of a metallo-\u03b2-lactamase in a member of the \u03b1 subdivision of the class<jats:italic>Proteobacteria<\/jats:italic>.<\/jats:p>","DOI":"10.1128\/aac.46.6.1823-1830.2002","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:09:29Z","timestamp":1027764569000},"page":"1823-1830","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":66,"title":["CAU-1, a Subclass B3 Metallo-\u03b2-Lactamase of Low Substrate Affinity Encoded by an Ortholog Present in the<i>Caulobacter crescentus<\/i>Chromosome"],"prefix":"10.1128","volume":"46","author":[{"given":"Jean-Denis","family":"Docquier","sequence":"first","affiliation":[{"name":"Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Universita\u0300 di Siena, 53100 Siena"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabrizio","family":"Pantanella","sequence":"additional","affiliation":[{"name":"Dipartimento di Sanita\u0300 Pubblica, Sezione di Microbiologia, Universita\u0300 di Roma \u201cLa Sapienza,\u201d 00185 Rome"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesco","family":"Giuliani","sequence":"additional","affiliation":[{"name":"Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Universita\u0300 di Siena, 53100 Siena"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria Cristina","family":"Thaller","sequence":"additional","affiliation":[{"name":"Dipartimento di Biologia, Universita\u0300 di Roma \u201cTor Vergata,\u201d 00133 Rome"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gianfranco","family":"Amicosante","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze e Tecnologie Biomediche, Universita\u0300 di L'Aquila, 67100 L'Aquila, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Moreno","family":"Galleni","sequence":"additional","affiliation":[{"name":"Laboratoire d'Enzymologie et Centre d'Inge\u0301nierie des Prote\u0301ines, Institut de Chimie, Universite\u0301 de Lie\u0300ge, Sart Tilman, B-4000 Lie\u0300ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Marie","family":"Fre\u0300re","sequence":"additional","affiliation":[{"name":"Laboratoire d'Enzymologie et Centre d'Inge\u0301nierie des Prote\u0301ines, Institut de Chimie, Universite\u0301 de Lie\u0300ge, Sart Tilman, B-4000 Lie\u0300ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen","family":"Bush","sequence":"additional","affiliation":[{"name":"RW Johnson Pharmaceutical Research Institute, Raritan, New Jersey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gian Maria","family":"Rossolini","sequence":"additional","affiliation":[{"name":"Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Universita\u0300 di Siena, 53100 Siena"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/aem.62.10.3557-3559.1996"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1098\/rstb.1980.0049"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.44.7.1878-1886.2000"},{"key":"e_1_3_2_5_2","first-page":"127","volume":"171","year":"1999","unstructured":"Bellais, S., S. 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