704906-46-7Relevant articles and documents
Glycosyltransferase activity can be selectively modulated by chemical modifications of acceptor substrates
Galan, M. Carmen,Dodson, Christopher S.,Venot, Andre P.,Boons, Geert-Jan
, p. 2205 - 2208 (2007/10/03)
A range of N-acetyllactosamine derivatives, which are modified by a wide range of functionalities at C-2′ and C-6, have been synthesised and the kinetic parameters of transfer catalysed by recombinant α-2,6-sialyltransferase and α-1,3-fucoyltra
The design and synthesis of a selective inhibitor of fucosyltransferase VI.
Galan, M Carmen,Venot, Andre P,Phillips, Robert S,Boons, Geert-Jan
, p. 1376 - 1380 (2007/10/03)
Inversion of configuration of the C-2[prime or minute] hydroxyl of methyl N-acetyllactosamine was accomplished by a two-step procedure involving oxidation to a ketone followed by reduction with NaBH(4). After deprotection, the resulting derivative was examined as a substrate for [small alpha]-(2,6)- and [small alpha]-(2,3)-sialyltransferase and fucosyltransferase III, IV, V and VI. It was found that none of these enzymes could glycosylate. However, it showed exquisite selectivity for inhibition of fucosyltransferase VI. The kinetic data support an unusual mechanism in which the inhibitor can bind to the GDP-fucose complex as well as another enzyme form.