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
ChemInform Abstract: Synthesis of a New Transition-State Analogue of the Sialyl Donor. Inhibition of Sialyltransferases.
โ Scribed by Hongbin Sun; Jingsong Yang; Katie E. Amaral; Benjamin A. Horenstein
- Publisher
- John Wiley and Sons
- Year
- 2010
- Weight
- 32 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0931-7597
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โฆ Synopsis
Abstract
ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a โFull Textโ option. The original article is trackable via the โReferencesโ option.
๐ SIMILAR VOLUMES
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 ยฑ 6)-sialyltransferase from rat liver (EC 2.4.99.1) only moderate inhibition was found for these compounds. In order to obtain transitio
## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a โFull Textโ option. The original article is trackable v