From Substrate to Transition State Analogues: The First Potent Inhibitor of Sialyltransferases
✍ Scribed by Peer Nils Schröder; Athanassios Giannis
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 77 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0044-8249
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📜 SIMILAR VOLUMES
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 cyt
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
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