The Substrate Specificity of Amyloglucosidase (AMG). Part IV. Hydroxycyclohexyl Glucosides.
- 1 January 1989
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 43 (4) , 373-380
- https://doi.org/10.3891/acta.chem.scand.43-0373
Abstract
Cyclohexyl- and (1R,2R)- and (1S, 2S)-hydroxycyclohexyl .alpha.-D-glucosides have been synthesized under halide-catalysed glycosylation reaction conditions. Furthermore, phenyl and 2-hydroxyphenyl .alpha.-D-glucopyranosides have been synthesised using fusion reactions in 60-70% yield. Finally, methyl 4-O-(.beta.-L-galactopyranosyl)-.beta.-D-glucopyranoside has been prepared in high yield using silver triflate-promoted glycosylation conditions. All compounds have been characterised by NMR spectroscopy and their preferred solution conformations inferred from the NMR data and hardsphere exo-anomeric effect calculations (HSEA). All the above-mentioned compounds have been investigated as potential substrates for the enzyme amyloglucosidase (AMG). The results show that only the compounds which have a preferred ground-state conforation similar to that of maltose can act as substrates for the enzyme.This publication has 2 references indexed in Scilit:
- The Substrate Specificity of the Enzyme Amyloglucosidase (AMG). Part II. 6-Substituted Maltose Derivatives.Acta Chemica Scandinavica, 1988
- Neutron diffraction refinement of the crystal structures of methyl α-D-galactopyranoside monohydrate and methyl β-D-galactopyranosideActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1979