The Substrate Specificity of the Enzyme Amyloglucosidase (AMG). Part I. Deoxy Derivatives
| Autor: | Klaus Bock, Henrik Pedersen, Karin M. O. Lundbäck, Erik B. Pedersen |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
chemistry.chemical_classification
Magnetic Resonance Spectroscopy biology Stereochemistry General Chemical Engineering Disaccharide Glycoside Substrate (chemistry) Nuclear magnetic resonance spectroscopy Substrate Specificity Kinetics chemistry.chemical_compound Enzyme chemistry Hydrolase biology.protein Amylase Glucan 1 4-alpha-Glucosidase Maltose Spectroscopy Glucosidases |
| Zdroj: | Acta Chemica Scandinavica. :617-628 |
| ISSN: | 0904-213X |
| DOI: | 10.3891/acta.chem.scand.41b-0617 |
| Popis: | The eight possible monodeoxy derivatives of methyl beta-maltoside and two bisdeoxy derivatives have been synthesized. The unprotected glycosides have all been investigated by NMR (1H and 13C) spectroscopy in order to confirm their structures and to obtain supporting information about their preferred solution conformations. The compounds have all been tested as substrates toward the hydrolase, amyloglucosidase (AMG) and it has been demonstrated that three hydroxy groups (3, 4' and 6') are essential for the compounds to act as substrate for the enzyme. The kinetic parameters KM (Michaelis-Menten constant) and VM (maximum rate for the reaction) have been determined using 1H NMR spectroscopy at 500 MHz. |
| Databáze: | OpenAIRE |
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