Premium
A Glycosyltransferase Inhibitor from a Molecular Fragment Library Simultaneously Interferes with Metal Ion and Substrate Binding
Author(s) -
Jørgensen Rene,
Grimm Lena Lisbeth,
Sindhuwinata Nora,
Peters Thomas,
Palcic Monica M.
Publication year - 2012
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/anie.201108345
Subject(s) - glycosyltransferase , substrate (aquarium) , fragment (logic) , chemistry , metal , substrate specificity , stereochemistry , combinatorial chemistry , enzyme , biochemistry , biology , computer science , organic chemistry , ecology , programming language
A fragmented approach : 3‐Phenyl‐5‐piperazino‐1,2,4‐thiadiazole (designated “compound 382” in the Ro5 Maybridge Fragment Library, see scheme) is demonstrated to be an effective inhibitor of human blood group glycosyltransferase B. The compound interferes with both acceptor and donor binding and also displaces the Mn 2+ ion in the binding pocket.