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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 916 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 907 | - |
dc.citation.title | MOLECULAR MICROBIOLOGY | - |
dc.citation.volume | 60 | - |
dc.contributor.author | Kim, JY | - |
dc.contributor.author | Jung, HI | - |
dc.contributor.author | An, YJ | - |
dc.contributor.author | Hun, JH | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Lee, HS | - |
dc.contributor.author | Lee, SH | - |
dc.contributor.author | Cha, SS | - |
dc.date.accessioned | 2023-12-22T10:06:47Z | - |
dc.date.available | 2023-12-22T10:06:47Z | - |
dc.date.created | 2014-09-02 | - |
dc.date.issued | 2006-05 | - |
dc.description.abstract | The emergence and dissemination of extended-spectrum (ES) β-lactamases induce therapeutic failure and a lack of eradication of clinical isolates even by third-generation β-lactam antibiotics like ceftazidime. CMY-10 is a plasmid-encoded class C β-lactamase with a wide spectrum of substrates. Unlike the well-studied class C ES β-lactamase from Enterobacter cloacae GC1, the Ω-loop does not affect the active site conformation and the catalytic activity of CMY-10. Instead, a three-amino-acid deletion in the R2-loop appears to be responsible for the ES activity of CMY-10. According to the crystal structure solved at 1.55 A resolution, the deletion significantly widens the R2 active site, which accommodates the R2 side-chains of β-lactam antibiotics. This observation led us to demonstrate the hydrolysing activity of CMY-10 towards imipenem with a long R2 substituent. The forced mutational analyses of P99 β-lactamase reveal that the introduction of deletion mutations into the R2-loop is able to extend the substrate spectrum of class C non-ES β-lactamases, which is compatible with the isolation of natural class C ES enzymes harbouring deletion mutations in the R2-loop. Consequently, the opening of the R2 active site by the deletion of some residues in the R2-loop can be considered as an operative molecular strategy of class C β-lactamases to extend their substrate spectrum. | - |
dc.identifier.bibliographicCitation | MOLECULAR MICROBIOLOGY, v.60, no.4, pp.907 - 916 | - |
dc.identifier.doi | 10.1111/j.1365-2958.2006.05146.x | - |
dc.identifier.issn | 0950-382X | - |
dc.identifier.scopusid | 2-s2.0-33646436194 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/5669 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33646436194 | - |
dc.identifier.wosid | 000237297800009 | - |
dc.language | 영어 | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.title | Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | TRANSITION-STATE ANALOG | - |
dc.subject.keywordPlus | ENTEROBACTER-CLOACAE P99 | - |
dc.subject.keywordPlus | CLINICAL ISOLATE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | OMEGA-LOOP | - |
dc.subject.keywordPlus | INHIBITOR DESIGN | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | RESISTANCE | - |
dc.subject.keywordPlus | ACID | - |
dc.subject.keywordPlus | MUTAGENESIS | - |
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