Sterol 14-demethylase

Sterol 14-demethylase (also known as CYP51) is an enzyme that is encoded by the CYP51 gene in humans. It is a member of the cytochrome P450 superfamily of enzymes, which are monooxygenases that catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, and other lipids.

Etymology[edit | edit source]

The term "sterol 14-demethylase" is derived from the function of the enzyme. "Sterol" refers to any of a group of naturally occurring unsaturated steroid alcohols, typically waxy solids. "14-demethylase" indicates the enzyme's function of removing a methyl group from the 14th carbon atom in the sterol molecule.

Function[edit | edit source]

Sterol 14-demethylase is involved in the biosynthesis of sterols. It catalyzes the removal of the 14α-methyl group from lanosterol, a critical step in the biosynthesis of cholesterol in humans and ergosterol in fungi. This reaction is one of the most complex of all those catalyzed by P450s, involving an initial hydroxylation of the 14α-methyl group, followed by a second oxidation to form the 14α-carboxyaldehyde, and a third oxidation to form the 14α-carboxylic acid, which is finally removed as formic acid.

Clinical significance[edit | edit source]

Inhibitors of sterol 14-demethylase have been shown to be effective in the treatment of certain fungal infections. Drugs such as fluconazole and itraconazole are examples of sterol 14-demethylase inhibitors. These drugs inhibit the production of ergosterol, a critical component of the fungal cell membrane, leading to the death of the fungus.

References[edit | edit source]

Sterol 14-demethylase Resources
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