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dc.contributor.author차선신*
dc.date.accessioned2017-05-30T01:05:21Z-
dc.date.available2017-05-30T01:05:21Z-
dc.date.issued2017*
dc.identifier.issn0066-4804*
dc.identifier.issn1098-6596*
dc.identifier.otherOAK-20575*
dc.identifier.urihttps://dspace.ewha.ac.kr/handle/2015.oak/235204-
dc.description.abstractNucleotides were effective in inhibiting the class C beta-lactamase CMY-10. IMP was the most potent competitive inhibitor, with a K-i value of 16.2 mu M. The crystal structure of CMY-10 complexed with GMP or IMP revealed that nucleotides fit into the R2 subsite of the active site with a unique vertical binding mode where the phosphate group at one terminus is deeply bound in the subsite and the base at the other terminus faces the solvent.*
dc.languageEnglish*
dc.publisherAMER SOC MICROBIOLOGY*
dc.subjectGMP*
dc.subjectIMP*
dc.subjectbeta-lactamases*
dc.subjectcompetitive inhibitor*
dc.titleGMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C beta-Lactamase*
dc.typeArticle*
dc.relation.issue5*
dc.relation.volume61*
dc.relation.indexSCIE*
dc.relation.indexSCOPUS*
dc.relation.journaltitleANTIMICROBIAL AGENTS AND CHEMOTHERAPY*
dc.identifier.doi10.1128/AAC.00098-17*
dc.identifier.wosidWOS:000403532100010*
dc.identifier.scopusid2-s2.0-85018186854*
dc.author.googleNa, Jung-Hyun*
dc.author.googleAn, Young Jun*
dc.author.googleCha, Sun-Shin*
dc.contributor.scopusid차선신(7201864593)*
dc.date.modifydate20240429134916*


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