{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T18:59:36Z","timestamp":1792004376055,"version":"4.4.0"},"reference-count":0,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[1994,1,1]],"date-time":"1994-01-01T00:00:00Z","timestamp":757382400000},"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":[[1994,1]]},"abstract":"<jats:p>A clinical isolate of Serratia marcescens (TN9106) produced a metallo beta-lactamase (IMP-1) which conferred resistance to imipenem and broad-spectrum beta-lactams. The blaIMP gene providing imipenem resistance was cloned and expressed in Escherichia coli HB101. The IMP-1 was purified from E. coli HB101 that harbors pSMBNU24 carrying blaIMP, and its apparent molecular mass was calculated to be about 30 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Kinetic studies of IMP-1 against various beta-lactams revealed that this enzyme hydrolyzes not only various broad-spectrum beta-lactams but also carbapenems. However, aztreonam was relatively stable against IMP-1. Although clavulanate or cloxacillin failed to inhibit IMP-1, Hg2+, Fe2+, or Cu2+ blocked the enzyme's activity. Moreover, the presence of EDTA in the reaction buffer resulted in a decrease in the enzyme's activity. Carbapenem resistance was not transferred from S. marcescens TN9106 to E. coli CSH2 by conjugation. A hybridization study confirmed that blaIMP was encoded on the chromosome of S. marcescens TN9106. By nucleotide sequencing analysis, blaIMP was found to encode a protein of 246 amino acid residues and was shown to have considerable homology to the metallo beta-lactamase genes of Bacillus cereus, Bacteroides fragilis, and Aeromonas hydrophila. The G+C content of blaIMP was 39.4%. Four consensus amino acid residues, His-95, His-97, Cys-176, and His-215, which form putative zinc ligands, were conserved in the deduced amino acid sequence of IMP-1. By determination of the amino acid sequence at the N terminus of purified mature IMP-1, 18 amino acid residues were found to be processed from the N terminus of the premature enzyme as a signal peptide. These results clearly show that IMP-1 is an enterobacterial metallo beta-lactamase, of which the primary structure has been completely determined, that confers resistance to carbapenems and other broad-spectrum beta-lactams.<\/jats:p>","DOI":"10.1128\/aac.38.1.71","type":"journal-article","created":{"date-parts":[[2012,6,28]],"date-time":"2012-06-28T00:05:50Z","timestamp":1340841950000},"page":"71-78","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":383,"title":["Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance"],"prefix":"10.1128","volume":"38","author":[{"given":"E","family":"Osano","sequence":"first","affiliation":[{"name":"Department of Bacteriology, Nagoya University School of Medicine, Japan."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Y","family":"Arakawa","sequence":"additional","affiliation":[{"name":"Department of Bacteriology, Nagoya University School of Medicine, Japan."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R","family":"Wacharotayankun","sequence":"additional","affiliation":[{"name":"Department of Bacteriology, Nagoya University School of Medicine, Japan."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Ohta","sequence":"additional","affiliation":[{"name":"Department of Bacteriology, Nagoya University School of Medicine, Japan."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"T","family":"Horii","sequence":"additional","affiliation":[{"name":"Department of Bacteriology, Nagoya University School of Medicine, Japan."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H","family":"Ito","sequence":"additional","affiliation":[{"name":"Department of Bacteriology, Nagoya University School of Medicine, Japan."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F","family":"Yoshimura","sequence":"additional","affiliation":[{"name":"Department of Bacteriology, Nagoya University School of Medicine, Japan."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N","family":"Kato","sequence":"additional","affiliation":[{"name":"Department of Bacteriology, Nagoya University School of Medicine, Japan."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","container-title":["Antimicrobial Agents and Chemotherapy"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.38.1.71","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.38.1.71","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,21]],"date-time":"2022-02-21T15:35:45Z","timestamp":1645457745000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/AAC.38.1.71"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1994,1]]}},"alternative-id":["10.1128\/AAC.38.1.71"],"URL":"https:\/\/doi.org\/10.1128\/aac.38.1.71","relation":{},"ISSN":["0066-4804","1098-6596"],"issn-type":[{"value":"0066-4804","type":"print"},{"value":"1098-6596","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,1]]},"assertion":[{"value":"1994-01-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}