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dc.contributor.authorXu, Guogangen_US
dc.contributor.authorKiefel, Miltonen_US
dc.contributor.authorWilson, Jennyen_US
dc.contributor.authorW. Andrew, Peteren_US
dc.contributor.authorR. Oggioni, Marcoen_US
dc.contributor.authorL. Taylor, Garryen_US
dc.contributor.editorPeter J. Stangen_US
dc.date.accessioned2017-05-03T12:19:12Z
dc.date.available2017-05-03T12:19:12Z
dc.date.issued2011en_US
dc.identifier.issn00027863en_US
dc.identifier.doi10.1021/ja110733qen_US
dc.identifier.urihttp://hdl.handle.net/10072/42125
dc.description.abstractStreptococcus penumoniae is a major human pathogen responsible for respiratory tract infections, septicemia, and meningitis and continues to produce numerous cases of disease with relatively high mortalities. S. pneumoniae encodes up to three sialidases, NanA, NanB, and NanC, that have been implicated in pathogenesis and are potential drug targets. NanA has been shown to be a promiscuous sialidase, hydrolyzing the removal of Neu5Ac from a variety of glycoconjugates with retention of configuration at the anomeric center, as we confirm by NMR. NanB is an intramolecular trans-sialidase producing 2,7-anhydro-Neu5Ac selectively from R2,3-sialosides. Here, we show that the first product of NanC is 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en) that can be slowly hydrated by the enzyme to Neu5Ac. We propose that the three pneumococcal sialidases share a common catalytic mechanism up to the final product formation step, and speculate on the roles of the enzymes in the lifecycle of the bacterium.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_US
dc.format.extent222188 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglishen_US
dc.language.isoen_US
dc.publisherAmerican Chemical Societyen_US
dc.publisher.placeUnited Statesen_US
dc.relation.ispartofstudentpublicationNen_US
dc.relation.ispartofpagefrom1718en_US
dc.relation.ispartofpageto1721en_US
dc.relation.ispartofissue6en_US
dc.relation.ispartofjournalJournal of the American Chemical Societyen_US
dc.relation.ispartofvolume133en_US
dc.rights.retentionYen_US
dc.subject.fieldofresearchProteins and Peptidesen_US
dc.subject.fieldofresearchcode030406en_US
dc.titleThree Streptococcus pneumoniae Sialidases: Three Different Productsen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.rights.copyrightThis document is the unedited Author’s version of a Submitted Work that was subsequently accepted for publication in Journal of the American Chemical Society, copyright 2011American Chemical Society after peer review. To access the final edited and published work see http://dx.doi.org/10.1021/ja110733q.en_US
gro.date.issued2015-09-04T04:34:19Z
gro.hasfulltextFull Text


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