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
Research output: Contribution to journal › Journal article › Research › peer-review
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.
| Original language | English |
|---|---|
| Journal | Bioorganic & Medicinal Chemistry |
| Volume | 12 |
| Issue number | 13 |
| Pages (from-to) | 3485-95 |
| Number of pages | 11 |
| ISSN | 0968-0896 |
| DOIs | |
| Publication status | Published - 1 Jul 2004 |
- Binding, Competitive, Enzyme Inhibitors, Imino Pyranoses, Mannitol, Molecular Structure, Rhizobium, Structure-Activity Relationship, beta-Glucosidase
Research areas
ID: 158554721