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From Substrate to Transition State Analogues: The First Potent Inhibitor of Sialyltransferases
Author(s) -
Schröder Peer Nils,
Giannis Athanassios
Publication year - 1999
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19990517)38:10<1379::aid-anie1379>3.0.co;2-m
Subject(s) - sialyltransferase , glycoconjugate , substrate (aquarium) , substrate specificity , sialic acid , chemistry , enzyme , stereochemistry , transition (genetics) , rational design , transition state analog , biochemistry , combinatorial chemistry , active site , biology , nanotechnology , materials science , ecology , gene
An important tool for exploring the biological functions of sialic acid containing glycoconjugates is compound 1 , created by the rational design reported by R. R. Schmidt et al. Compound 1 inhibits α (2‐6)‐sialyltransferase with a K i value of 40 n M and thus exhibits a 1000‐fold higher affinity for the enzyme than the natural substrate.