Abstract
The activity of 7-deoxyloganin 7-hydroxylase, an enzyme catalyzing the conversion of 7-deoxyloganin into loganin, was detected in a microsomal preparation from the cell suspension cultures of Lonicera japonica. It was dependent on NADPH and molecular oxygen. The enzymatic reaction was inhibited by carbon monoxide as well as by several cytochrome P450 inhibitors, especially ketoconazole, indicating that the reaction was mediated by cytochrome P450. The enzyme showed substrate specificity for 7-deoxyloganin. The K(m) values for 7-deoxyloganin and NADPH were estimated as 170 and 18 microM, respectively, from Lineweaver-Burk plots.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Carbon Monoxide / pharmacology
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Cells, Cultured
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Cytochrome P-450 Enzyme Inhibitors
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Enzyme Inhibitors / pharmacology
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Glucosides / metabolism
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Iridoids*
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Ketoconazole / pharmacology
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Magnoliopsida / enzymology*
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Metyrapone / pharmacology
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Miconazole / pharmacology
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Microsomes / enzymology
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Mixed Function Oxygenases / metabolism*
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NADP / metabolism
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Oxygen / metabolism
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Oxygen Consumption
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Pyrans / metabolism
Substances
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Cytochrome P-450 Enzyme Inhibitors
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Enzyme Inhibitors
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Glucosides
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Iridoids
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Pyrans
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NADP
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Miconazole
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Carbon Monoxide
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Mixed Function Oxygenases
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7-Deoxyloganin 7-hydroxylase
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loganin
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Ketoconazole
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Oxygen
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Metyrapone