Role of the side chain of lanosterol in substrate recognition and catalytic activity of lanosterol 14α-demethylase (cytochrome P-45014DM) of yeast
Author:
Publisher
Elsevier BV
Subject
Endocrinology,Biochemistry,Biophysics
Reference17 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. Evidence for the presence of cytochrome P-450 functional in lanosterol 14α-demethylation in microsomes of aerobically grown respiring yeast
4. Microsomal enzymes of cholesterol biosynthesis. Purification of lanosterol 14 alpha-methyl demethylase cytochrome P-450 from hepatic microsomes.
5. 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.
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