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Issue 6, 2016
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Inhibition of the key enzyme of sialic acid biosynthesis by C6-Se modified N-acetylmannosamine analogs

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Abstract

Synthetically accessible C6-analogs of N-acetylmannosamine (ManNAc) were tested as potential inhibitors of the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase (GNE/MNK), the key enzyme of sialic acid biosynthesis. Enzymatic experiments revealed that the modification introduced at the C6 saccharide position strongly influences the inhibitory potency. A C6-ManNAc diselenide dimer showed the strongest kinase inhibition in the low μM range among all the substrates tested and successfully reduced cell surface sialylation in Jurkat cells.

Graphical abstract: Inhibition of the key enzyme of sialic acid biosynthesis by C6-Se modified N-acetylmannosamine analogs

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Supplementary files

Article information


Submitted
27 Oct 2015
Accepted
13 Feb 2016
First published
19 Feb 2016

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2016,7, 3928-3933
Article type
Edge Article

Inhibition of the key enzyme of sialic acid biosynthesis by C6-Se modified N-acetylmannosamine analogs

O. Nieto-Garcia, P. R. Wratil, L. D. Nguyen, V. Böhrsch, S. Hinderlich, W. Reutter and C. P. R. Hackenberger, Chem. Sci., 2016, 7, 3928
DOI: 10.1039/C5SC04082E

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