A 1H STD NMR spectroscopic investigation of sialylnucleoside mimetics as probes of CMP-Kdn synthetase

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Title A 1H STD NMR spectroscopic investigation of sialylnucleoside mimetics as probes of CMP-Kdn synthetase
Author Haselhorst, Thomas Erwin; Oschlies, Melanie; Abu-Izneid, Tareq; Kiefel, Milton; Tiralongo, Giuseppe; Münster-Kühnel, Anja K.; Gerardy-Schahn, Rita; von Itzstein, Mark
Journal Name Glycoconjugate Journal
Year Published 2006
Place of publication United States
Publisher Springer
Abstract 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 Sialylnucleoside mimetics, where the sialic acid moiety has been replaced by a carboxyl group and a hydrophobic moiety, have been used in NMR experiments, to probe the tolerance of the CMP-Kdn synthetase to such replacements.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.
Peer Reviewed Yes
Published Yes
Alternative URI http://dx.doi.org/10.1007/s10719-006-6735-y
Volume 23
Issue Number 5/6
Page from 371
Page to 375
ISSN 0282-0080
Date Accessioned 2007-02-23
Date Available 2010-08-26T07:37:35Z
Language en_AU
Research Centre Institute for Glycomics
Faculty Institute for Glycomics
Subject PRE2009-Biochemistry and Cell Biology; PRE2009-Enzymes; PRE2009-Medical Biochemistry: Carbohydrates
URI http://hdl.handle.net/10072/13719
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1

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