{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T09:15:38Z","timestamp":1790241338264,"version":"4.1.0"},"reference-count":29,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2000,11,1]],"date-time":"2000-11-01T00:00:00Z","timestamp":973036800000},"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":[[2000,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            VIM-1 is a new group 3 metallo-\u03b2-lactamase recently detected in carbapenem-resistant nosocomial isolates of\n            <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n            from the Mediterranean area. In this work, VIM-1 was purified from an\n            <jats:italic>Escherichia coli<\/jats:italic>\n            strain carrying the cloned\n            <jats:italic>bla<\/jats:italic>\n            <jats:sub>VIM-1<\/jats:sub>\n            gene by means of an anion-exchange chromatography step followed by a gel permeation chromatography step. The purified enzyme exhibited a molecular mass of 26 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and an acidic pI of 5.1 in analytical isoelectric focusing. Amino-terminal sequencing showed that mature VIM-1 results from the removal of a 26-amino-acid signal peptide from the precursor. VIM-1 hydrolyzes a broad array of \u03b2-lactam compounds, including penicillins, narrow- to expanded-spectrum cephalosporins, carbapenems, and mechanism-based serine-\u03b2-lactamase inactivators. Only monobactams escape hydrolysis. The highest catalytic constant\/\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            ratios (&gt;10\n            <jats:sup>6<\/jats:sup>\n            M\n            <jats:sup>\u22121<\/jats:sup>\n            \u00b7 s\n            <jats:sup>\u22121<\/jats:sup>\n            ) were observed with carbenicillin, azlocillin, some cephalosporins (cephaloridine, cephalothin, cefuroxime, cefepime, and cefpirome), imipenem, and biapenem. Kinetic parameters showed remarkable variability with different \u03b2-lactams and also within the various penam, cephem, and carbapenem compounds, resulting in no clear preference of the enzyme for any of these \u03b2-lactam subfamilies. Significant differences were observed with some substrates between the kinetic parameters of VIM-1 and those of other metallo-\u03b2-lactamases. Inactivation assays carried out with various chelating agents (EDTA, 1,10-\n            <jats:italic>o<\/jats:italic>\n            -phenanthroline, and pyridine-2,6-dicarboxylic acid) indicated that formation of a ternary enzyme-metal-chelator complex precedes metal removal from the zinc center of the protein and revealed notable differences in the inactivation parameters of VIM-1 with different agents.\n          <\/jats:p>","DOI":"10.1128\/aac.44.11.3003-3007.2000","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:06:42Z","timestamp":1027764402000},"page":"3003-3007","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":79,"title":["Purification and Biochemical Characterization of the VIM-1 Metallo-\u03b2-Lactamase"],"prefix":"10.1128","volume":"44","author":[{"given":"Nicola","family":"Franceschini","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Dipartimento di Scienze e Tecnologie Biomediche, Universita\u0300 degli Studi L'Aquila, I-67100 Coppito, L'Aquila,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Berardo","family":"Caravelli","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Dipartimento di Scienze e Tecnologie Biomediche, Universita\u0300 degli Studi L'Aquila, I-67100 Coppito, L'Aquila,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Denis","family":"Docquier","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Dipartimento di Biologia Molecolare, Sez. di Microbiologia, Universita\u0300 di Siena, I-53100 Siena,2 Italy, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Moreno","family":"Galleni","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->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, Belgium3"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Marie","family":"Fre\u0300re","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->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, Belgium3"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gianfranco","family":"Amicosante","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Dipartimento di Scienze e Tecnologie Biomediche, Universita\u0300 degli Studi L'Aquila, I-67100 Coppito, L'Aquila,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gian Maria","family":"Rossolini","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Dipartimento di Biologia Molecolare, Sez. di Microbiologia, Universita\u0300 di Siena, I-53100 Siena,2 Italy, and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.7.1612"},{"key":"e_1_3_3_3_2","first-page":"127","article-title":"Molecular characterization of a carbapenem-hydrolyzing \u03b2-lactamase from Chryseobacterium (Flavobacterium) indologenes.","volume":"171","author":"Bellais S.","year":"1999","unstructured":"Bellais S. 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