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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

Authors :
Wrodnigg, Tanja M
Diness, Frederik
Gruber, Christoph
Häusler, Herwig
Lundt, Inge
Rupitz, Karen
Steiner, Andreas J
Stütz, Arnold E
Tarling, Chris A
Withers, Stephen G
Wölfler, Heidrun
Wrodnigg, Tanja M
Diness, Frederik
Gruber, Christoph
Häusler, Herwig
Lundt, Inge
Rupitz, Karen
Steiner, Andreas J
Stütz, Arnold E
Tarling, Chris A
Withers, Stephen G
Wölfler, Heidrun
Source :
Wrodnigg , T M , Diness , F , Gruber , C , Häusler , H , Lundt , I , Rupitz , K , Steiner , A J , Stütz , A E , Tarling , C A , Withers , S G & Wölfler , H 2004 , ' 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 ' , Bioorganic & Medicinal Chemistry , vol. 12 , no. 13 , pp. 3485-95 .
Publication Year :
2004

Abstract

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.

Details

Database :
OAIster
Journal :
Wrodnigg , T M , Diness , F , Gruber , C , Häusler , H , Lundt , I , Rupitz , K , Steiner , A J , Stütz , A E , Tarling , C A , Withers , S G & Wölfler , H 2004 , ' 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 ' , Bioorganic & Medicinal Chemistry , vol. 12 , no. 13 , pp. 3485-95 .
Notes :
English
Publication Type :
Electronic Resource
Accession number :
edsoai.on1316694948
Document Type :
Electronic Resource