ABSTRACT
Insight into the structure and inhibition mechanism of O-ß-d-glucosidases by deoxa-pyranosylamine type inhibitors is provided by X-ray analysis of complexes between raucaffricine and strictosidine glucosidases and N-(cyclohexylmethyl)-, N-(cyclohexyl)- and N-(bromobenzyl)-ß-d-gluco-1,5-deoxa-pyranosylamine. All inhibitors anchored exclusively in the catalytic active site by competition with appropriate enzyme substrates. Thus facilitated prospective elucidation of the binding networks with residues located at <3.9 Å distance will enable the development of potent inhibitors suitable for the production of valuable alkaloid glucosides, raucaffricine and strictosidine, by means of synthesis in Rauvolfia serpentina cell suspension cultures.
Subject(s)
Cyclopentanes/pharmacology , Glucosidases/antagonists & inhibitors , Glucosidases/metabolism , Sugar Alcohols/pharmacology , Binding Sites/drug effects , Cyclopentanes/chemistry , Dose-Response Relationship, Drug , Glucosidases/chemistry , Ligands , Models, Molecular , Molecular Structure , Rauwolfia/cytology , Rauwolfia/enzymology , Structure-Activity Relationship , Sugar Alcohols/chemistryABSTRACT
The attachment of multiple triazole moieties and perfluoroalkyl chains to TEMPO promotes emulsion formation in dichloromethane/water, giving a highly active and easily recoverable catalyst for the oxidation of alcohols.
