Lanosterol 14α-demethylase. Similarity of the enzyme system from yeast and rat liver
Autor: | Konstantinos A. Mitropoulos, Bernard E.A. Reeves, Geoffrey F. Gibbons |
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Rok vydání: | 1976 |
Předmět: |
Chemical Phenomena
Formates Stereochemistry Formic acid Clinical Biochemistry Saccharomyces cerevisiae In Vitro Techniques Biology Biochemistry Lanosterol chemistry.chemical_compound Endocrinology Cytochrome P-450 Enzyme System Species Specificity Biosynthesis Ergosterol mental disorders polycyclic compounds Animals Molecular Biology Pharmacology Carbon Monoxide Cholesterol Organic Chemistry Yeast Rats Chemistry Kinetics chemistry Microsomes Liver Microsome biology.protein Demethylase lipids (amino acids peptides and proteins) Oxidoreductases |
Zdroj: | Steroids. 27:821-829 |
ISSN: | 0039-128X |
Popis: | The chemical synthesis of 24,25-dihydro[32-14C]lanosterol is described. The incubation of this material with a cell-free system from Saccharomvoes cerevisiae or with a microsomal preparation from rat liver resulted in both cases in the release of [14C]formic acid. This result suggests that in the biosynthesis of ergosterol in yeast, as well as in that of cholesterol in higher animals, the 14α-methyl group of lanosterol is removed as formic acid. In both systems, the measurement of the rate of release of [14C]formic acid from 24,25-dihydro[32-14C]lanosterol provides a simple and direct assay of lanosterol 14α-demethylase. Carbon monoxide inhibited both yeast and liver 14α-demethylase. |
Databáze: | OpenAIRE |
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