The 3-hydroxy group of lanosterol is essential for orienting the substrate site of cytochrome P-450(14DM) (lanosterol 14 alpha- demethylase) |
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| Authors: | Y Aoyama Y Yoshida Y Sonoda Y Sato |
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| Institution: | Faculty of Pharmaceutical Sciences, Mukogawa Women's University, Nishinomiya, Japan. |
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| Abstract: | Interaction of lanosterol, 3-epilanosterol, 3-oxolanosta-8,24-diene, 3-methylenelanost-8-ene and lanosterol acetate with cytochrome P-450(14DM) were studied. The cytochrome mediated the 14alpha-demethylation of 3-epilanosterol with nearly the same activity as lanosterol but could not mediate the 14alpha-demethylation of the 3-methylene derivative and the 3-acetate. The cytochrome catalyzed the 14alpha-demethylation of the 3-oxo derivative with low rate. Based on these and some additional observations the hydrogen bond formation between the 3-hydroxy group of lanosterol and the specific amino acid residue in the substrate site is assumed to be essential for orienting the substrate in the substrate site of the cytochrome. |
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