Utilize este identificador para referenciar este registo: http://hdl.handle.net/10773/25114
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dc.contributor.authorFonseca, Fátimapt_PT
dc.contributor.authorArthur, Christopher J.pt_PT
dc.contributor.authorBromley, Elizabeth H. C.pt_PT
dc.contributor.authorSamyn, Bartpt_PT
dc.contributor.authorMoerman, Pablopt_PT
dc.contributor.authorSaavedra, Maria Josépt_PT
dc.contributor.authorCorreia, Antóniopt_PT
dc.contributor.authorSpencer, Jamespt_PT
dc.date.accessioned2019-01-15T14:20:59Z-
dc.date.available2019-01-15T14:20:59Z-
dc.date.issued2011-
dc.identifier.issn0066-4804pt_PT
dc.identifier.urihttp://hdl.handle.net/10773/25114-
dc.description.abstractThe subclass B2 metallo-β-lactamase (MBL) Sfh-I from Serratia fonticola UTAD54 was cloned and overexpressed in Escherichia coli. The recombinant protein binds one equivalent of zinc, as shown by mass spectrometry, and preferentially hydrolyzes carbapenem substrates. However, compared to other B2 MBLs, Sfh-I also shows limited hydrolytic activity against some additional substrates and is not inhibited by a second equivalent of zinc. These data confirm Sfh-I to be a subclass B2 metallo-β-lactamase with some distinctive properties.pt_PT
dc.language.isoengpt_PT
dc.publisherAmerican Society for Microbiologypt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F30490%2F2006/PTpt_PT
dc.rightsopenAccesspt_PT
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/pt_PT
dc.titleBiochemical characterization of Sfh-I, a subclass B2 metallo-β-Lactamase from a Serratia fonticola UTAD54pt_PT
dc.typearticlept_PT
dc.description.versionpublishedpt_PT
dc.peerreviewedyespt_PT
degois.publication.firstPage5392pt_PT
degois.publication.issue11pt_PT
degois.publication.lastPage5395pt_PT
degois.publication.titleAntimicrobial Agents and Chemotherapypt_PT
degois.publication.volume55pt_PT
dc.identifier.doi10.1128/AAC.00429-11pt_PT
dc.identifier.essn1098-6596pt_PT
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