Show simple item record

dc.contributor.authorHaselhorst, T
dc.contributor.authorMunster-Kuhnel, AK
dc.contributor.authorStolz, A
dc.contributor.authorOschlies, M
dc.contributor.authorTiralongo, J
dc.contributor.authorKitajima, K
dc.contributor.authorGerardy-Schahn, R
dc.contributor.authorvon Itzstein, M
dc.date.accessioned2017-05-03T14:16:57Z
dc.date.available2017-05-03T14:16:57Z
dc.date.issued2005
dc.date.modified2009-10-19T05:25:00Z
dc.identifier.issn0006-291X
dc.identifier.doi10.1016/j.bbrc.2004.12.040
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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeAmsterdam
dc.publisher.urihttp://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description#description
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom565
dc.relation.ispartofpageto570
dc.relation.ispartofissue2
dc.relation.ispartofjournalBiochemical and Biophysical Research Communications
dc.relation.ispartofvolume327
dc.rights.retentionY
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchMedical Biochemistry and Metabolomics
dc.subject.fieldofresearchcode0304
dc.subject.fieldofresearchcode0601
dc.subject.fieldofresearchcode1101
dc.titleProbing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2005
gro.hasfulltextNo Full Text
gro.griffith.authorvon Itzstein, Mark
gro.griffith.authorHaselhorst, Thomas E.
gro.griffith.authorTiralongo, Joe


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