کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10771927 | 1050845 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Probing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
CMP-Kdn synthetase catalyses the reaction of sialic acids (Sia) and cytidine-5â²-triphosphate (CTP) to the corresponding activated sugar nucleotide CMP-Sia and pyrophosphate PPi. STD NMR experiments of a recombinant nucleotide cytidine-5â²-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 1H 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 31P NMR spectroscopy was successfully used to follow the enzyme reaction and clearly confirmed the appearance of CMP-Sia and the inorganic pyrophosphate by-product.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 327, Issue 2, 11 February 2005, Pages 565-570
Journal: Biochemical and Biophysical Research Communications - Volume 327, Issue 2, 11 February 2005, Pages 565-570
نویسندگان
Thomas Haselhorst, Anja K. Münster-Kühnel, Anita Stolz, Melanie Oschlies, Joe Tiralongo, Ken Kitajima, Rita Gerardy-Schahn, Mark von Itzstein,