Probing the aglycon binding site of a beta-glucosidase: a collection of C-1-modified 2,5-dideoxy-2,5-imino-D-mannitol derivatives and their structure-activity relationships as competitive inhibitors.
A range of new C-1 modified derivatives of the powerful glucosidase inhibitor 2,5-dideoxy-2,5-imino-D-mannitol has been synthesised and their biological activities probed with the beta-glucosidase from Agrobacterium sp. Ki values are compared with those of previously prepared close relatives. Findings suggest dramatic effects exerted by the aglycon binding site on substrate/inhibitor binding.
Wrodnigg
Tanja M
TM
Glycogroup, Institut für Organische Chemie, Technische Universität Graz, Stremayrgasse 16, A-8010 Graz, Austria.
Diness
Frederik
F
Gruber
Christoph
C
Häusler
Herwig
H
Lundt
Inge
I
Rupitz
Karen
K
Steiner
Andreas J
AJ
Stütz
Arnold E
AE
Tarling
Chris A
CA
Withers
Stephen G
SG
Wölfler
Heidrun
H
D001667:Binding, Competitive; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D050112:Imino Pyranoses; D008353:Mannitol / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D015394:Molecular Structure; D012231:Rhizobium / Q000187:drug effects / Q000201:enzymology; D013329:Structure-Activity Relationship; D001617:beta-Glucosidase / Q000737:chemistry* / Q000378:metabolism*
C494911:2,5-dideoxy-2,5-imino-D-mannitol; D004791:Enzyme Inhibitors; D050112:Imino Pyranoses; D008353:Mannitol; D001617:beta-Glucosidase