Deformylation of 32-oxo-24,25-dihydrolanosterol by the purified cytochrome P-45014DM (lanosterol 14 α-demethylase) from yeast evidence confirming the intermediate step of lanosterol 14 α-demethylation-Reference-Cited by-同舟云学术

Deformylation of 32-oxo-24,25-dihydrolanosterol by the purified cytochrome P-45014DM (lanosterol 14 α-demethylase) from yeast evidence confirming the intermediate step of lanosterol 14 α-demethylation

Published:1989-11 Issue:31 Volume:264 Page:18502-18505
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Aoyama Y,Yoshida Y,Sonoda Y,Sato Y

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

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. Microsomal enzymes of cholesterol biosynthesis. Purification of lanosterol 14 alpha-methyl demethylase cytochrome P-450 from hepatic microsomes.

4. Lanosterol 14α-demethylase. Similarity of the enzyme system from yeast and rat liver

5. The 14α—demethylation of lanosterol by a reconstituted cytochrome P-450 system from yeast microsomes

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