10.1021/jo0525682.s001
Régis Fauré
Régis
Fauré
Marc Saura-Valls
Marc
Saura-Valls
Harry Brumer
Harry
Brumer
Antoni Planas
Antoni
Planas
Sylvain Cottaz
Sylvain
Cottaz
Hugues Driguez
Hugues
Driguez
Synthesis of a Library of Xylogluco-Oligosaccharides for Active-Site
Mapping of Xyloglucan <i>endo</i>-Transglycosylase
American Chemical Society
2006
chemical synthesis
enzyme
Synthesi
oligosaccharide
degradation
compound
OH
yield
unsubstituted
terminal glucosyl units
fluoride
reaction product
Humicola insolens
donor synthon
enzymatically
residue
XET
plant cell wall biosynthesis
lactosyl motif
efficiency
acceptor
galactose
building blocks
synthesizing
Cel 7B E 197A glycosynthase
xyloglucan polymers
Constituting
site
target molecules
Mapping
modification
mapping
condensation
lactose
Xyloglucan
2006-07-07 00:00:00
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Synthesis_of_a_Library_of_Xylogluco_Oligosaccharides_for_Active_Site_Mapping_of_Xyloglucan_i_endo_i_Transglycosylase/3071878
Complex oligosaccharides containing α-d-xylosyl-(1→6)-β-d-glucosyl residues and unsubstituted β-(1→4)-linked d-glucosyl units were readily synthesized using enzymatic coupling catalyzed by the Cel7B E197A
glycosynthase from <i>Humicola insolens</i>. Constituting this library required four key steps: (1) preparing
unprotected building blocks by chemical synthesis or enzymatic degradation of xyloglucan polymers;
(2) generating the donor synthon in the enzymatic coupling by temporarily introducing a lactosyl motif
on the 4-OH of the terminal glucosyl units of the xylogluco-oligosaccharides; (3) synthesizing the
corresponding α-fluorides, followed by their de-<i>O</i>-acetylation and the glycosynthase-catalyzed condensation
of these donors onto various acceptors; and (4) enzymatically releasing lactose or galactose from the
reaction product, affording the target molecules in good overall yields. These complex oligosaccharides
proved useful for mapping the active site of a key enzyme in plant cell wall biosynthesis and
modification: the xyloglucan <i>endo</i>-transglycosylase (XET). We also report some preliminary enzymatic
results regarding the efficiency of these compounds.