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Probing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.

Abstract：

:CMP-Kdn synthetase catalyses the reaction of sialic acids (Sia) and cytidine-5'-triphosphate (CTP) to the corresponding activated sugar nucleotide CMP-Sia and pyrophosphate PP(i). 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 (1)H 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 (31)P NMR spectroscopy was successfully used to follow the enzyme reaction and clearly confirmed the appearance of CMP-Sia and the inorganic pyrophosphate by-product.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Haselhorst T,Münster-Kühnel AK,Stolz A,Oschlies M,Tiralongo J,Kitajima K,Gerardy-Schahn R,von Itzstein M

doi

10.1016/j.bbrc.2004.12.040

subject

Has Abstract

pub_date

2005-02-11 00:00:00

pages

565-70

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(04)02828-1

journal_volume

327

pub_type

杂志文章

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