Enzymatic sialyl transfer with CMP-Neu5Ac as donor can be inhibited by CDP. Therefore phosphonates 1 a,b, 2 and 3 were synthesized as substrate analogues. With a(2 ± 6)-sialyltransferase from rat liver (EC 2.4.99.1) only moderate inhibition was found for these compounds. In order to obtain transitio
Efficient Sialyltransferase Inhibitors Based on Transition-State Analogues of the Sialyl Donor
✍ Scribed by Bernd Müller; Christoph Schaub; Richard R. Schmidt
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 161 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0044-8249
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✦ Synopsis
A 200- to 1000-fold higher affinity for sialyltransferase is shown by compounds 1 and 2 relative to the natural substrate. These inhibitors, which are derived from the transition state of S 1-type sialyltransfer, contain a flat ring that is attached through a carbon atom with a phosphonate and a cytidine monophosphate group.
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