Show simple item record

dc.contributor.authorHaselhorst, Thomasen_US
dc.contributor.authorK. Muenster-Kuehnel, Anjaen_US
dc.contributor.authorStolz, Anitaen_US
dc.contributor.authorOschiles, Melanieen_US
dc.contributor.authorTiralongo, Joeen_US
dc.contributor.authorKitajima, Kenen_US
dc.contributor.authorGerardy-Schahn, Ritaen_US
dc.contributor.authorvon Itzstein, Marken_US
dc.date.accessioned2017-05-03T14:16:57Z
dc.date.available2017-05-03T14:16:57Z
dc.date.issued2005en_US
dc.date.modified2009-10-19T05:25:00Z
dc.identifier.issn0006291Xen_US
dc.identifier.doi10.1016/j.bbrc.2004.12.040en_AU
dc.identifier.urihttp://hdl.handle.net/10072/4183
dc.description.abstractCMP-Kdn synthetase catalyses the reaction of sialic acids (Sia) and cytidine-5'-triphosphate (CTP) to the corresponding activated sugar nucleotide CMP-Sia and pyrophosphate PPi. STD NMR experiments of a recombinant nucleotide cytidine-5'-monophosphate-3-deoxy-D-glycero-D-galacto-nonulosonic acid synthetase (CMP-Kdn synthetase) were performed to map the binding epitope of the substrate CTP and the product CMP-Neu5Ac. The STD NMR analysis clearly shows that the anomeric proton of the ribose moiety of both investigated compounds is in close proximity to the protein surface and is likely to play a key role in the binding process. The relative rates of the enzyme reaction, derived from 1H NMR signal integrals, show that Kdn is activated at a rate 2.5 and 3.1 faster than Neu5Ac and Neu5Gc, respectively. Furthermore, proton-decoupled 31P NMR spectroscopy was successfully used to follow the enzyme reaction and clearly confirmed the appearance of CMP-Sia and the inorganic pyrophosphate by-product.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevieren_US
dc.publisher.placeAmsterdamen_US
dc.publisher.urihttp://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description#descriptionen_AU
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom565en_US
dc.relation.ispartofpageto570en_US
dc.relation.ispartofissue2en_US
dc.relation.ispartofjournalBiochemical and Biophysical Research Communicationsen_US
dc.relation.ispartofvolume327en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchcode320302en_US
dc.titleProbing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.en_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2005
gro.hasfulltextNo Full Text


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record