Enzymatic synthesis of the glycosides of calystegines B1 and B2 and their glycosidase inhibitory activities
| Autor: | M.George Jones, Naoki Asano, Haruhisa Kizu, Katsuhiko Matsui, Alison A. Watson, Rhodri C. Griffiths, Atsushi Kato, Robert J. Nash |
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| Rok vydání: | 1997 |
| Předmět: |
Glycosylation
Magnetic Resonance Spectroscopy Glycoside Hydrolases Nortropanes Swine Cellobiose Solanaceous Alkaloids Biochemistry Analytical Chemistry Fungal Proteins chemistry.chemical_compound Non-competitive inhibition Animals Glycoside hydrolase Glycosides Enzyme Inhibitors Trehalase Plant Proteins chemistry.chemical_classification Organic Chemistry Rhodotorula Glycoside Oryza General Medicine Maltose Enzyme chemistry Cattle Glucosidases |
| Zdroj: | Carbohydrate Research. 304:173-178 |
| ISSN: | 0008-6215 |
| Popis: | Several glycosides of calystegines B1 and B2 were synthesized by use of rice alpha-glucosidase and the whole cells of Rhodotorula lactosa, and their glycosidase inhibitory activities were investigated. Incubation of mixture of calystegine B1 and maltose with rice alpha-glucosidase gave 3-O-alpha-D-glucopyranosylcalystegine B1 (2, 11.3%). An enzymatic beta-transglucosylation reaction of calystegines B1 or B2 with cellobiose using the whole cells of R. lactosa gave 3-O-beta-D-glucopyranosylcalystegine B1 (1) (0.9%) or 4-O-beta-D-glucopyranosylcalystegine B2 (3, 11.2%), respectively, while similar beta-transgalactosylation of calystegine B2 from lactose gave 4-O-beta-D-galactopyranosylcalystegine B2 (4, 10.1%). The glycosylation of calystegines B1 and B2 markedly decreased or abolished their inhibition against beta-glucosidase, alpha- or beta-galactosidase. Compound 4 however retained more or less the potency of calystegine B2 against trehalase. Interestingly, compound 1 was a noncompetitive inhibitor of rice alpha-glucosidase, with a Ki value of 0.9 +/- 0.1 microM. |
| Databáze: | OpenAIRE |
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