| A 1H STD NMR spectroscopic investigation of sialylnucleoside mimetics as probes of CMP-Kdn synthetase. | |
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MedLine Citation:
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PMID: 16897179 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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CMP-Kdn synthetase catalyses the reaction of sialic acids (Sia) and CTP to the corresponding activated sugar nucleotide CMP-Sia and pyrophosphate PP( i ). Saturation Transfer Difference (STD) NMR spectroscopy has been employed to investigate the sub-structural requirements of the enzyme's binding domain. Sialylnucleoside mimetics, where the sialic acid moiety has been replaced by a carboxyl group and a hydrophobic moiety, have been used in NMR experiments, to probe the tolerance of the CMP-Kdn synthetase to such replacements. From our data it would appear that unlike another sialylnucleotide-recognising protein, the CMP-Neu5Ac transport protein, either a phosphate group or other functional groups on the sialic acid framework may play important roles in recognition by the synthetase. |
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Authors:
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Thomas Haselhorst; Melanie Oschlies; Tareq Abu-Izneid; Milton J Kiefel; Joe Tiralongo; Anja K Münster-Kühnel; Rita Gerardy-Schahn; Mark von Itzstein |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Glycoconjugate journal Volume: 23 ISSN: 0282-0080 ISO Abbreviation: Glycoconj. J. Publication Date: 2006 Jul |
Date Detail:
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Created Date: 2006-08-09 Completed Date: 2007-10-31 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8603310 Medline TA: Glycoconj J Country: United States |
Other Details:
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Languages: eng Pagination: 371-5 Citation Subset: IM |
Affiliation:
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Institute for Glycomics, Griffith University (Gold Coast Campus), PMB 50 Gold Coast Mail Centre, Queensland 9726, Australia. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Carbohydrate Sequence Magnetic Resonance Spectroscopy* Molecular Mimicry* Molecular Probes / chemistry* Molecular Sequence Data N-Acetylneuraminic Acid / chemistry*, metabolism Nucleosides / chemistry*, metabolism Nucleotidyltransferases / chemistry* |
| Chemical | |
Reg. No./Substance:
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0/Molecular Probes; 0/Nucleosides; 131-48-6/N-Acetylneuraminic Acid; EC 2.7.7.-/CTP-CMP-3-deoxynonulosonate cytidyltransferase; EC 2.7.7.-/Nucleotidyltransferases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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