A 1H STD NMR spectroscopic investigation of sialylnucleoside mimetics as probes of CMP-Kdn synthetase.
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 Sialylnucleoside mimetics, where the sialic acid moiety has been replaced by a carboxyl group and a hydrophobic moiety, have been used in NMR experiments, to probe the tolerance of the CMP-Kdn synthetase to such replacements.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.
Haselhorst
Thomas
T
Institute for Glycomics, Griffith University (Gold Coast Campus), PMB 50 Gold Coast Mail Centre, Queensland 9726, Australia.
Oschlies
Melanie
M
Abu-Izneid
Tareq
T
Kiefel
Milton J
MJ
Tiralongo
Joe
J
Münster-Kühnel
Anja K
AK
Gerardy-Schahn
Rita
R
von Itzstein
Mark
M
D002240:Carbohydrate Sequence; D009682:Magnetic Resonance Spectroscopy; D018716:Molecular Mimicry; D015335:Molecular Probes / Q000737:chemistry*; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid / Q000737:chemistry* / Q000378:metabolism; D009705:Nucleosides / Q000737:chemistry* / Q000378:metabolism; D009713:Nucleotidyltransferases / Q000737:chemistry*
D015335:Molecular Probes; D009705:Nucleosides; C079494:CTP-CMP-3-deoxynonulosonate cytidyltransferase; D009713:Nucleotidyltransferases; D019158:N-Acetylneuraminic Acid