Acceptor substrate-based selective inhibition of galactosyltransferases.
This paper describes the discovery of glycosyl acceptor analogs as potent and selective inhibitors of alpha-1,3- and beta-1,4-galactosyltransferases. Incorporation of an appropriate aromatic group to the aglycon position of the enzyme's acceptors results in a strong inhibition, representing the first and most potent small uncharged molecules as selective inhibitors of these two enzymes and thus providing a new strategy for the development of selective glycosyltransferase inhibitors.
Chung
S J
SJ
Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037, USA.
Takayama
S
S
Wong
C H
CH
D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology; D005700:Galactosyltransferases / Q000037:antagonists & inhibitors*; D013329:Structure-Activity Relationship
D004791:Enzyme Inhibitors; D005700:Galactosyltransferases