A 1H STD NMR spectroscopic investigation of sialylnucleoside mimetics as probes of CMP-Kdn synthetase |
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Authors: | 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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Affiliation: | Institute for Glycomics, Griffith University (Gold Coast Campus), PMB 50 Gold Coast Mail Centre, Queensland 9726, Australia. |
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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 Sialylnucleoside mimetics, where the sialic acid moiety has been replaced by a carboxyl group and a hydrophobic moiety, have been used in NMR experiments, to probe the tolerance of the CMP-Kdn synthetase to such replacements.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. Dedicated to the memory of Professor Dr Yasuo Inoue |
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Keywords: | Nucleotide Synthetase Sialic Acids Sialic Acid mimetics NMR spectroscopy |
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