The 3-hydroxy group of lanosterol is essential for orienting the substrate in the substrate site of cytochrome P-45014DM (Lanosterol 14α-demethylase)
Author:
Publisher
Elsevier BV
Subject
Endocrinology,Biochemistry,Biophysics
Reference21 articles.
1. Yeast cytochrome P-450 catalyzing lanosterol 14 alpha-demethylation. I. Purification and spectral properties.
2. Yeast cytochrome P-450 catalyzing lanosterol 14 alpha-demethylation. II. Lanosterol metabolism by purified P-450(14)DM and by intact microsomes.
3. Metabolism of 32-hydroxy-24,25-dihydrolanosterol by purified cytochrome P-45014DM from yeast. Evidence for contribution of the cytochrome to whole process of lanosterol 14 alpha-demethylation.
4. Role of the 8-double bond of lanosterol in the enzyme-substrate interaction of cytochrome P-45014DM (lanosterol 14α-demethylase)
5. 7-Oxo-24,25-dihydrolanosterol: a novel lanosterol 14α-demethylase (P-45014DM) inhibitor which blocks electron transfer to the oxyferro intermediate
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2. Imidazolylchromanones containing alkyl side chain as lanosterol 14α-demethylase inhibitors: synthesis, antifungal activity and docking study;Journal of Enzyme Inhibition and Medicinal Chemistry;2013-03-14
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