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dc.contributor.authorHou, Chun-Feng D.
dc.contributor.authorPhelan, Emer K.
dc.contributor.authorMiraula, Manfredi
dc.contributor.authorOllis, David L.
dc.contributor.authorSchenk, Gerhard
dc.contributor.authorMitić, Nataša
dc.date.accessioned2016-10-17T08:52:40Z
dc.date.available2016-10-17T08:52:40Z
dc.date.issued2014-01
dc.identifier.citationAmerican Journal of Molecular Biology, 2014, 4, 11-15en_US
dc.identifier.urihttp://dx.doi.org/10.4236/ajmb.2014.41002
dc.identifier.urihttp://hdl.handle.net/123456789/959
dc.description.abstractMetallo-β-lactamases (MBLs) are a family of Zn2+-dependent enzymes that have contributed strongly to the emergence and spread of antibiotic resistance. Novel members as well as variants of existing members of this family are discovered continuously, compounding their threat to global health care. MBLs are divided into three subgroups, i.e. B1, B2 and B3. The recent discovery of an unusual MBL from Serratia proteamaculans (SPR-1) suggests the presence of an additional subgroup, i.e. B4. A database search reveals that SPR-1 has only one homologue from Cronobacter sakazakii, CSA-1.These two MBLs have a unique active site and may employ a mechanism distinct from other MBLs, but reminiscent of some organophosphate-degrading hydrolases.en_US
dc.language.isoenen_US
dc.publisherScientific Research Publishingen_US
dc.subjectAntibiotic Resistanceen_US
dc.subjectβ-Lactam Antibioticsen_US
dc.subjectMetallo-β-Lactamasesen_US
dc.subjectSequence Homologyen_US
dc.subjectSerratia proteamaculansen_US
dc.subjectCronobacter sakazakiien_US
dc.titleUnusual metallo-β-lactamases may constitute a new subgroup in this family of enzymesen_US
dc.typeArticleen_US


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