Calystegine B4, a novel trehalase inhibitor from Scopolia japonica
| Autor: | Katsuhiko Matsui, Haruhisa Kizu, Naoki Asano, Robert J. Nash, Alison A. Watson, Atsushi Kato |
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| Rok vydání: | 1996 |
| Předmět: |
Magnetic Resonance Spectroscopy
Glycoside Hydrolases Nortropanes Swine Stereochemistry Kidney Binding Competitive Solanaceous Alkaloids Biochemistry Gas Chromatography-Mass Spectrometry Analytical Chemistry chemistry.chemical_compound Alkaloids Carbohydrate Conformation Animals Trehalase Enzyme Inhibitors chemistry.chemical_classification Molecular Structure biology Plant Extracts Alkaloid Organic Chemistry Tropane General Medicine Plants biology.organism_classification Yeast Rats Intestines Kinetics Enzyme chemistry Scopolia japonica Tropane alkaloid Solanaceae Tropanes |
| Zdroj: | Carbohydrate Research. 293:195-204 |
| ISSN: | 0008-6215 |
| DOI: | 10.1016/0008-6215(96)00204-2 |
| Popis: | GLC-MS analysis has been developed for screening plants of the family Solanaceae for new calystegines. GLC-MS analyses of the extract of Scopolia japonica showed the presence of a new tetrahydroxy- nor -tropane alkaloid in addition to the known calystegines A 3 , A 5 , B 1 , B 2 , B 3 , and C 1 . We gave this new alkaloid the trivial name calystegine B 4 . The structure of calystegine B 4 was determined as 1α,2β,3α,4α-tetrahydroxy- nor -tropane from a variety of NMR spectral data. Calystegines B 1 , B 2 , and C 1 are potent competitive inhibitors with K i values ranging from 10 −6 to 10 −7 M for almond β-glucosidase, while calystegine B 4 inhibited this enzyme in a competitive manner, with a K i value of 7.3 μM. Calystegine B 2 is also a potent inhibitor of green coffee bean α-galactosidase, whereas calystegine B 4 exhibited no significant activity for this enzyme. Among rat intestinal glycosidases, only trehalase was potently inhibited by calystegine B 4 , with an IC 50 value of 9.8 μM. Furthermore, calystegine B 4 potently inhibited pig kidney trehalase in a competitive manner, with a K i value of 1.2 μM, but it was almost inactive against yeast and fungal trehalases. |
| Databáze: | OpenAIRE |
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